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.


1u99

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u99.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1u99.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u99| PDB=1u99 | SCENE= }}
{{STRUCTURE_1u99| PDB=1u99 | SCENE= }}
-
'''"Crystal Structures of E. coli RecA in a Compressed Helical Filament Form 4"'''
+
==="Crystal Structures of E. coli RecA in a Compressed Helical Filament Form 4"===
-
==Overview==
+
<!--
-
The X-ray crystal structure of uncomplexed Escherichia coli RecA protein has been determined in three new crystal forms at resolutions of 1.9 A, 2.0 A, and 2.6 A. The RecA protein used for this study contains the extra residues Gly-Ser-His-Met at the N terminus, but retains normal ssDNA-dependent ATPase and coprotease activities. In all three crystals, RecA is packed in a right-handed helical filament with a pitch of approximately 74 A. These RecA filaments are compressed relative to the original crystal structure of RecA, which has a helical pitch of 82.7 A. In the structures of the compressed RecA filament, the monomer-monomer interface and the core domain are essentially the same as in the RecA structure with the 83 A pitch. The change in helical pitch is accommodated by a small movement of the N-terminal domain, which is reoriented to preserve the contacts it makes at the monomer-monomer interface. The new crystal structures show significant variation in the orientation and conformation of the C-terminal domain, as well as in the inter-filament packing interactions. In crystal form 2, a calcium ion is bound closely to a beta-hairpin of the C-terminal domain and to Asp38 of a neighboring filament, and residues 329-331 of the C-terminal tail become ordered to contact a neighboring filament. In crystal forms 3 and 4, a sulfate ion or a phosphate anion is bound to the same site on RecA as the beta-phosphate group of ADP, causing an opening of the P-loop. Altogether, the structures show the conformational variability of RecA protein in the crystalline state, providing insight into many aspects of RecA function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15364575}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15364575 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15364575}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Hoomologous recombination]]
[[Category: Hoomologous recombination]]
[[Category: Reca]]
[[Category: Reca]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:55:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:22:38 2008''

Revision as of 23:22, 28 July 2008

Image:1u99.png

Template:STRUCTURE 1u99

"Crystal Structures of E. coli RecA in a Compressed Helical Filament Form 4"

Template:ABSTRACT PUBMED 15364575

About this Structure

1U99 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of Escherichia coli RecA in a compressed helical filament., Xing X, Bell CE, J Mol Biol. 2004 Oct 1;342(5):1471-85. PMID:15364575

Page seeded by OCA on Tue Jul 29 02:22:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u99"
Personal tools