2hp7: Difference between revisions

Revision as of 21:39, 27 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:2hp7.png

Template:STRUCTURE 2hp7

Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motorStructure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor

Template:ABSTRACT PUBMED 16882724

About this StructureAbout this Structure

2HP7 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor., Park SY, Lowder B, Bilwes AM, Blair DF, Crane BR, Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11886-91. Epub 2006 Aug 1. PMID:16882724

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-[[Image:2hp7.gif|left|200px]]
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-'''Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor'''
+===Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor===
-==Overview==
+<!--
-Bacteria switch the direction their flagella rotate to control movement. FliM, along with FliN and FliG, compose a complex in the motor that, upon binding phosphorylated CheY, reverses the sense of flagellar rotation. The 2.0-A resolution structure of the FliM middle domain (FliM(M)) from Thermotoga maritima reveals a pseudo-2-fold symmetric topology similar to the CheY phosphatases CheC and CheX. A variable structural element, which, in CheC, mediates binding to CheD (alpha2') and, in CheX, mediates dimerization (beta'(x)), has a truncated structure unique to FliM (alpha2'). An exposed helix of FliM(M) (alpha1) does not contain the catalytic residues of CheC and CheX but does include positions conserved in FliM sequences. Cross-linking experiments with site-directed cysteine mutants show that FliM self-associates through residues on alpha1 and alpha2'. CheY activated by BeF(3)(-) binds to FliM with approximately 40-fold higher affinity than CheY (K(d) = 0.04 microM vs. 2 microM). Mapping residue conservation, suppressor mutation sites, binding data, and deletion analysis onto the FliM(M) surface defines regions important for contacts with the stator-interacting protein FliG and for either counterclockwise or clockwise rotation. Association of 33-35 FliM subunits would generate a 44- to 45-nm-diameter disk, consistent with the known dimensions of the C-ring. The localization of counterclockwise- and clockwise-biasing mutations to distinct surfaces suggests that the binding of phosphorylated CheY cooperatively realigns FliM around the ring.
+The line below this paragraph, {{ABSTRACT_PUBMED_16882724}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16882724 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16882724}}
 ==About this Structure==
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 [[Category: Bacterial chemotaxis]]
 [[Category: Flagellar switch complex]]
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