This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sx1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sx1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1sx1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sx1| PDB=1sx1 | SCENE= }}
{{STRUCTURE_1sx1| PDB=1sx1 | SCENE= }}
-
'''Solution NMR Structure and X-ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15260479}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15260479 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15260479}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SX1 OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SX1 OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Tetrahedral coordination]]
[[Category: Tetrahedral coordination]]
[[Category: Zinc]]
[[Category: Zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:14:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:30:55 2008''

Revision as of 14:31, 27 July 2008

Template:STRUCTURE 1sx1

Solution NMR Structure and X-ray Absorption Analysis of the C-Terminal Zinc-Binding Domain of the SecA ATPase

Template:ABSTRACT PUBMED 15260479

About this Structure

Full experimental 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

Page seeded by OCA on Sun Jul 27 17:30:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools