1jmw
From Proteopedia
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| - | [[Image:1jmw.jpg|left|200px]] | + | [[Image:1jmw.jpg|left|200px]] |
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| - | '''Propagating Conformational Changes Over Long (And Short) Distances''' | + | {{Structure |
| + | |PDB= 1jmw |SIZE=350|CAPTION= <scene name='initialview01'>1jmw</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Propagating Conformational Changes Over Long (And Short) Distances''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JMW is a [ | + | 1JMW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11504940 11504940] |
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''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 12:05:35 2008'' |
Revision as of 10:05, 20 March 2008
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| , resolution 1.9Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 12:05:35 2008
