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1jmw
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmw OCA], [http://www.ebi.ac.uk/pdbsum/1jmw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jmw RCSB]</span> | ||
}} | }} | ||
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[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:56 2008'' |
Revision as of 18:35, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Propagating Conformational Changes Over Long (And Short) Distances
Overview
The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.
About this Structure
1JMW is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Propagating conformational changes over long (and short) distances in proteins., Yu EW, Koshland DE Jr, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9517-20. PMID:11504940
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