View source for 1sx0


==Solution NMR Structure and X-Ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase==
<StructureSection load='1sx0' size='340' side='right'caption='[[1sx0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sx0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SX0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sx0 OCA], [https://pdbe.org/1sx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1sx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sx0 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The solution NMR structure of a 22-residue Zn(2+)-binding domain (ZBD) from Esherichia coli preprotein translocase subunit SecA is presented. In conjunction with X-ray absorption analysis, the NMR structure shows that three cysteines and a histidine in the sequence CXCXSGX(8)CH assume a tetrahedral arrangement around the Zn(2+) atom, with an average Zn(2+)-S bond distance of 2.30 A and a Zn(2+)-N bond distance of 2.03 A. The NMR structure shows that ND1 of His20 binds to the Zn(2+) atom. The ND1-Zn(2+) bond is somewhat strained: it makes an angle of approximately 17 degrees with the plane of the ring, and it also shows a significant "in-plane" distortion of 13 degrees. A comprehensive sequence alignment of the SecA-ZBD from many different organisms shows that, along with the four Zn(2+) ligands, there is a serine residue (Ser12) that is completely conserved. The NMR structure indicates that the side chain of this serine residue forms a strong hydrogen bond with the thiolate of the third cysteine residue (Cys19); therefore, the conserved serine appears to have a critical role in the structure. SecB, an export-specific chaperone, is the only known binding partner for the SecA-ZBD. A phylogenetic analysis using 86 microbial genomes shows that 59 of the organisms carry SecA with a ZBD, but only 31 of these organisms also possess a gene for SecB, indicating that there may be uncharacterized binding partners for the SecA-ZBD.

Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPase.,Dempsey BR, Wrona M, Moulin JM, Gloor GB, Jalilehvand F, Lajoie G, Shaw GS, Shilton BH Biochemistry. 2004 Jul 27;43(29):9361-71. PMID:15260479<ref>PMID:15260479</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1sx0" style="background-color:#fffaf0;"></div>

==See Also==
*[[SecA|SecA]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Dempsey BR]]
[[Category: Gloor GB]]
[[Category: Jalilehvand F]]
[[Category: Lajoie G]]
[[Category: Moulin JM]]
[[Category: Shaw GS]]
[[Category: Shilton BH]]
[[Category: Wrona M]]