2ibm

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{{Seed}}
 
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[[Image:2ibm.png|left|200px]]
 
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==A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA==
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The line below this paragraph, containing "STRUCTURE_2ibm", creates the "Structure Box" on the page.
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<StructureSection load='2ibm' size='340' side='right'caption='[[2ibm]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ibm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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{{STRUCTURE_2ibm| PDB=2ibm | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ibm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibm OCA], [https://pdbe.org/2ibm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibm RCSB], [https://www.ebi.ac.uk/pdbsum/2ibm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SECA_BACSU SECA_BACSU] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2ibm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ibm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The SecA ATPase moves polypeptides post-translationally across the plasma membrane of eubacteria, but the mechanism of transport is still unclear. We describe the crystal structure of a novel dimeric form of Bacillus subtilis SecA. Dimerization of SecA occurs at the prominent groove formed by the nucleotide binding domain 2 (nbd2) and the preprotein cross-linking (ppx) domain. The dimer interface is very large, burying approximately 5400 A(2) of solvent accessible surface per monomer. Single cysteine disulfide cross-linking shows the presence of this novel SecA dimer in solution. In addition, other dimers also exist in solution, arguing that they all are in equilibrium with monomeric SecA and supporting the idea that the monomer may be the functional species. Dimerization of SecA causes an alpha-helix of one subunit to convert to a short beta-strand that participates in beta-sheet formation with strands in the other subunit. This conversion of secondary structure elements occurs close to the connection between the nbd1 and ppx domains, a potential site of interaction with translocation substrate. Comparing the different X-ray structures of B. subtilis SecA suggests that small changes in the nucleotide binding domains could be amplified via helix 1 of the helical scaffold domain (hsd) to generate larger movements of the domains involved in polypeptide binding.
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===A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA===
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A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA.,Zimmer J, Li W, Rapoport TA J Mol Biol. 2006 Dec 1;364(3):259-65. Epub 2006 Aug 22. PMID:16989859<ref>PMID:16989859</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ibm" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16989859}}, adds the Publication Abstract to the page
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*[[Preprotein translocase|Preprotein translocase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16989859 is the PubMed ID number.
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*[[SecA|SecA]]
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== References ==
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{{ABSTRACT_PUBMED_16989859}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2IBM is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBM OCA].
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==Reference==
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<ref group="xtra">PMID:16989859</ref><references group="xtra"/>
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Li, W.]]
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[[Category: Large Structures]]
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[[Category: Rapoport, T A.]]
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[[Category: Li W]]
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[[Category: Zimmer, J.]]
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[[Category: Rapoport TA]]
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[[Category: Protein translocation]]
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[[Category: Zimmer J]]
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[[Category: Seca]]
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[[Category: Signal peptide binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:13:54 2009''
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Current revision

A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA

PDB ID 2ibm

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