2ch4
From Proteopedia
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[[Image:2ch4.png|left|200px]] | [[Image:2ch4.png|left|200px]] | ||
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{{STRUCTURE_2ch4| PDB=2ch4 | SCENE= }} | {{STRUCTURE_2ch4| PDB=2ch4 | SCENE= }} | ||
===COMPLEX BETWEEN BACTERIAL CHEMOTAXIS HISTIDINE KINASE CHEA DOMAINS P4 AND P5 AND RECEPTOR-ADAPTOR PROTEIN CHEW=== | ===COMPLEX BETWEEN BACTERIAL CHEMOTAXIS HISTIDINE KINASE CHEA DOMAINS P4 AND P5 AND RECEPTOR-ADAPTOR PROTEIN CHEW=== | ||
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{{ABSTRACT_PUBMED_16622408}} | {{ABSTRACT_PUBMED_16622408}} | ||
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==See Also== | ==See Also== | ||
| - | *[[Acetylcholinesterase]] | + | *[[Acetylcholinesterase|Acetylcholinesterase]] |
| + | *[[Chemotaxis protein|Chemotaxis protein]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016622408</ref><ref group="xtra">PMID:021110513</ref><references group="xtra"/> |
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Bilwes, A M.]] | [[Category: Bilwes, A M.]] | ||
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[[Category: Signal transduction]] | [[Category: Signal transduction]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
| + | [[Category: Transferase-chemotaxis complex]] | ||
[[Category: Transferase/chemotaxis]] | [[Category: Transferase/chemotaxis]] | ||
Revision as of 00:39, 27 July 2012
Contents |
COMPLEX BETWEEN BACTERIAL CHEMOTAXIS HISTIDINE KINASE CHEA DOMAINS P4 AND P5 AND RECEPTOR-ADAPTOR PROTEIN CHEW
Template:ABSTRACT PUBMED 16622408
About this Structure
2ch4 is a 4 chain structure of Acetylcholinesterase with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
See Also
Reference
- Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR. Reconstruction of the chemotaxis receptor-kinase assembly. Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:16622408 doi:10.1038/nsmb1085
- Erbse AH, Berlinberg AJ, Cheung CY, Leung WY, Falke JJ. OS-FRET: a new one-sample method for improved FRET measurements. Biochemistry. 2011 Feb 1;50(4):451-7. Epub 2010 Dec 30. PMID:21110513 doi:10.1021/bi101188b
