1sx0
From Proteopedia
(New page: 200px<br /><applet load="1sx0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sx0" /> '''Solution NMR Structure and X-Ray Absorption ...) |
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'''Solution NMR Structure and X-Ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase'''<br /> | '''Solution NMR Structure and X-Ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution NMR structure of a 22-residue Zn(2+)-binding domain (ZBD) | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1SX0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1SX0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SX0 OCA]. |
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15260479 15260479] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15260479 15260479] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Dempsey, B | + | [[Category: Dempsey, B R.]] |
| - | [[Category: Gloor, G | + | [[Category: Gloor, G B.]] |
[[Category: Jalilehvand, F.]] | [[Category: Jalilehvand, F.]] | ||
[[Category: Lajoie, G.]] | [[Category: Lajoie, G.]] | ||
| - | [[Category: Moulin, J | + | [[Category: Moulin, J M.]] |
| - | [[Category: Shaw, G | + | [[Category: Shaw, G S.]] |
| - | [[Category: Shilton, B | + | [[Category: Shilton, B H.]] |
[[Category: Wrona, M.]] | [[Category: Wrona, M.]] | ||
[[Category: metal ion]] | [[Category: metal ion]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:06:30 2008'' |
Revision as of 13:06, 21 February 2008
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Solution NMR Structure and X-Ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase
Overview
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.
About this Structure
1SX0 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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