1prr

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[[Image:1prr.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1prr| PDB=1prr | SCENE= }}
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|RELATEDENTRY=[[1prs|1PRS]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://www.ebi.ac.uk/pdbsum/1prr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB]</span>
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'''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM'''
'''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM'''
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[[Category: Ikura, M.]]
[[Category: Ikura, M.]]
[[Category: Inouye, S.]]
[[Category: Inouye, S.]]
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[[Category: binding protein]]
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[[Category: Binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:24:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:38 2008''
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Revision as of 02:24, 3 May 2008

Template:STRUCTURE 1prr

NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM


Overview

BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.

About this Structure

1PRR is a Single protein structure of sequence from Myxococcus xanthus. Full crystallographic information is available from OCA.

Reference

NMR-derived three-dimensional solution structure of protein S complexed with calcium., Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M, Structure. 1994 Feb 15;2(2):107-22. PMID:8081742 Page seeded by OCA on Sat May 3 05:24:45 2008

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