Evidence of mineralization activity and supramolecular assembly by the N-terminal sequence of ACCBP, a biomineralization protein that is homologous to the acetylcholine binding protein family

Fairland F. Amos, Moise Ndao, John Evans

Research output: Contribution to journalArticle

Abstract

Several biomineralization proteins that exhibit intrinsic disorder also possess sequence regions that are homologous to nonmineral associated folded proteins. One such protein is the amorphous calcium carbonate binding protein (ACCBP), one of several proteins that regulate the formation of the oyster shell and exhibit 30% conserved sequence identity to the acetylcholine binding protein sequences. To gain a better understanding of the ACCBP protein, we utilized bioinformatic approaches to identify the location of disordered and folded regions within this protein. In addition, we synthesized a 50 AA polypeptide, ACCN, representing the N-terminal domain of the mature processed ACCBP protein. We then utilized this polypeptide to determine the mineralization activity and qualitative structure of the N-terminal region of ACCBP. Our bioinformatic studies indicate that ACCBP consists of a ten-stranded β-sandwich structure that includes short disordered sequence blocks, two of which reside within the primarily helical and surface-accessible ACCN sequence. Circular dichroism studies reveal that ACCN is partially disordered in solution; however, ACCN can be induced to fold into an R helix in the presence of TFE. Furthermore, we confirm that the ACCN sequence is multifunctional; this sequence promotes radial calcite polycrystal growth on Kevlar threads and forms supramolecular assemblies in solution that contain amorphous-appearing deposits. We conclude that the partially disordered ACCN sequence is a putative site for mineralization activity within the ACCBP protein and that the presence of short disordered sequence regions within the ACCBP fold are essential for function.

Original languageEnglish (US)
Pages (from-to)3298-3305
Number of pages8
JournalBiomacromolecules
Volume10
Issue number12
DOIs
StatePublished - Dec 14 2009

Fingerprint

Biomineralization
Calcium Carbonate
Calcium carbonate
Acetylcholine
Carrier Proteins
Proteins
Polypeptides
Bioinformatics
Peptides
Sandwich structures
Calcite
Polycrystals
Polytetrafluoroethylene
Dichroism
Deposits

ASJC Scopus subject areas

  • Bioengineering
  • Materials Chemistry
  • Polymers and Plastics
  • Biomaterials

Cite this

@article{230cf6cb4e3c4ab5b0ecfc8a0f3f8cf6,
title = "Evidence of mineralization activity and supramolecular assembly by the N-terminal sequence of ACCBP, a biomineralization protein that is homologous to the acetylcholine binding protein family",
abstract = "Several biomineralization proteins that exhibit intrinsic disorder also possess sequence regions that are homologous to nonmineral associated folded proteins. One such protein is the amorphous calcium carbonate binding protein (ACCBP), one of several proteins that regulate the formation of the oyster shell and exhibit 30{\%} conserved sequence identity to the acetylcholine binding protein sequences. To gain a better understanding of the ACCBP protein, we utilized bioinformatic approaches to identify the location of disordered and folded regions within this protein. In addition, we synthesized a 50 AA polypeptide, ACCN, representing the N-terminal domain of the mature processed ACCBP protein. We then utilized this polypeptide to determine the mineralization activity and qualitative structure of the N-terminal region of ACCBP. Our bioinformatic studies indicate that ACCBP consists of a ten-stranded β-sandwich structure that includes short disordered sequence blocks, two of which reside within the primarily helical and surface-accessible ACCN sequence. Circular dichroism studies reveal that ACCN is partially disordered in solution; however, ACCN can be induced to fold into an R helix in the presence of TFE. Furthermore, we confirm that the ACCN sequence is multifunctional; this sequence promotes radial calcite polycrystal growth on Kevlar threads and forms supramolecular assemblies in solution that contain amorphous-appearing deposits. We conclude that the partially disordered ACCN sequence is a putative site for mineralization activity within the ACCBP protein and that the presence of short disordered sequence regions within the ACCBP fold are essential for function.",
author = "Amos, {Fairland F.} and Moise Ndao and John Evans",
year = "2009",
month = "12",
day = "14",
doi = "10.1021/bm900893f",
language = "English (US)",
volume = "10",
pages = "3298--3305",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "12",

}

TY - JOUR

T1 - Evidence of mineralization activity and supramolecular assembly by the N-terminal sequence of ACCBP, a biomineralization protein that is homologous to the acetylcholine binding protein family

AU - Amos, Fairland F.

AU - Ndao, Moise

AU - Evans, John

PY - 2009/12/14

Y1 - 2009/12/14

N2 - Several biomineralization proteins that exhibit intrinsic disorder also possess sequence regions that are homologous to nonmineral associated folded proteins. One such protein is the amorphous calcium carbonate binding protein (ACCBP), one of several proteins that regulate the formation of the oyster shell and exhibit 30% conserved sequence identity to the acetylcholine binding protein sequences. To gain a better understanding of the ACCBP protein, we utilized bioinformatic approaches to identify the location of disordered and folded regions within this protein. In addition, we synthesized a 50 AA polypeptide, ACCN, representing the N-terminal domain of the mature processed ACCBP protein. We then utilized this polypeptide to determine the mineralization activity and qualitative structure of the N-terminal region of ACCBP. Our bioinformatic studies indicate that ACCBP consists of a ten-stranded β-sandwich structure that includes short disordered sequence blocks, two of which reside within the primarily helical and surface-accessible ACCN sequence. Circular dichroism studies reveal that ACCN is partially disordered in solution; however, ACCN can be induced to fold into an R helix in the presence of TFE. Furthermore, we confirm that the ACCN sequence is multifunctional; this sequence promotes radial calcite polycrystal growth on Kevlar threads and forms supramolecular assemblies in solution that contain amorphous-appearing deposits. We conclude that the partially disordered ACCN sequence is a putative site for mineralization activity within the ACCBP protein and that the presence of short disordered sequence regions within the ACCBP fold are essential for function.

AB - Several biomineralization proteins that exhibit intrinsic disorder also possess sequence regions that are homologous to nonmineral associated folded proteins. One such protein is the amorphous calcium carbonate binding protein (ACCBP), one of several proteins that regulate the formation of the oyster shell and exhibit 30% conserved sequence identity to the acetylcholine binding protein sequences. To gain a better understanding of the ACCBP protein, we utilized bioinformatic approaches to identify the location of disordered and folded regions within this protein. In addition, we synthesized a 50 AA polypeptide, ACCN, representing the N-terminal domain of the mature processed ACCBP protein. We then utilized this polypeptide to determine the mineralization activity and qualitative structure of the N-terminal region of ACCBP. Our bioinformatic studies indicate that ACCBP consists of a ten-stranded β-sandwich structure that includes short disordered sequence blocks, two of which reside within the primarily helical and surface-accessible ACCN sequence. Circular dichroism studies reveal that ACCN is partially disordered in solution; however, ACCN can be induced to fold into an R helix in the presence of TFE. Furthermore, we confirm that the ACCN sequence is multifunctional; this sequence promotes radial calcite polycrystal growth on Kevlar threads and forms supramolecular assemblies in solution that contain amorphous-appearing deposits. We conclude that the partially disordered ACCN sequence is a putative site for mineralization activity within the ACCBP protein and that the presence of short disordered sequence regions within the ACCBP fold are essential for function.

UR - http://www.scopus.com/inward/record.url?scp=72449200669&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=72449200669&partnerID=8YFLogxK

U2 - 10.1021/bm900893f

DO - 10.1021/bm900893f

M3 - Article

C2 - 19904951

AN - SCOPUS:72449200669

VL - 10

SP - 3298

EP - 3305

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 12

ER -