1eqq: Difference between revisions

Revision as of 01:43, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1eqq.png

Template:STRUCTURE 1eqq

SINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEXSINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEX

Template:ABSTRACT PUBMED 10731701

About this StructureAbout this Structure

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

ReferenceReference

Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-Ray structure analysis., Matsumoto T, Morimoto Y, Shibata N, Kinebuchi T, Shimamoto N, Tsukihara T, Yasuoka N, J Biochem. 2000 Feb;127(2):329-35. PMID:10731701

Page seeded by OCA on Tue Jul 1 01:43:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1eqq.gif|left|200px]]
+{{Seed}}
+[[Image:1eqq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1eqq|  PDB=1eqq  |  SCENE=  }}
-'''SINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEX'''
+===SINGLE STRANDED DNA BINDING PROTEIN AND SSDNA COMPLEX===
-==Overview==
+<!--
-The single-stranded DNA (ssDNA) binding protein from Escherichia coli (EcoSSB) plays a central role in DNA replication, recombination and repair. The tertiary structure of EcoSSB was determined at 2.2 A resolution. This is rather higher resolution than previously reported. Crystals were grown from the homogeneous intact protein but the EcoSSB tetramer in the crystals contains truncated subunits lacking a part of the C-terminal. The structure determined includes biologically important flexible loops and C-terminal regions, and revealed the existence of concavities. These concavities include the residues important for ssDNA binding. An ssDNA can be fitted on the concavities and further stabilized through interactions with the loops forming flexible lids. It seems likely to play a central role in the binding of ssDNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_10731701}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10731701 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10731701}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Beta barrel]]
 [[Category: Protein-dna complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:25:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:43:42 2008''