1prr: Difference between revisions

Revision as of 00:50, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1prr.png

Template:STRUCTURE 1prr

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

Template:ABSTRACT PUBMED 8081742

About this StructureAbout this Structure

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

ReferenceReference

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 Tue Jul 29 00:50:21 2008

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OCA

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-[[Image:1prr.gif|left|200px]]
+{{Seed}}
+[[Image:1prr.png|left|200px]]
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 {{STRUCTURE_1prr|  PDB=1prr  |  SCENE=  }}
-'''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8081742}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8081742 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8081742}}
 ==About this Structure==
-PRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA].
+PRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA].
 ==Reference==
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 [[Category: Inouye, S.]]
 [[Category: Binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:24:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:50:21 2008''