1prr: Difference between revisions
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[[Image:1prr.gif|left|200px]] | [[Image:1prr.gif|left|200px]] | ||
'''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM''' | {{Structure | ||
|PDB= 1prr |SIZE=350|CAPTION= <scene name='initialview01'>1prr</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PRR is a [ | 1PRR 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8081742 8081742] | ||
[[Category: Myxococcus xanthus]] | [[Category: Myxococcus xanthus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: binding protein]] | [[Category: binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:06 2008'' | ||
Revision as of 11:28, 20 March 2008
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| Ligands: | CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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