2vko: Difference between revisions

Revision as of 16:33, 29 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:2vko.png

Template:STRUCTURE 2vko

STRUCTURE OF THE SOLUBLE DOMAIN OF THE MEMBRANE PROTEIN TM1634 FROM THERMOTOGA MARITIMASTRUCTURE OF THE SOLUBLE DOMAIN OF THE MEMBRANE PROTEIN TM1634 FROM THERMOTOGA MARITIMA

Template:ABSTRACT PUBMED 18369189

About this StructureAbout this Structure

2VKO is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634., McCleverty CJ, Columbus L, Kreusch A, Lesley SA, Protein Sci. 2008 Mar 27;. PMID:18369189

Page seeded by OCA on Tue Jul 29 16:33:55 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2vko.jpg|left|200px]]
+{{Seed}}
+[[Image:2vko.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2vko|  PDB=2vko  |  SCENE=  }}
-'''STRUCTURE OF THE SOLUBLE DOMAIN OF THE MEMBRANE PROTEIN TM1634 FROM THERMOTOGA MARITIMA'''
+===STRUCTURE OF THE SOLUBLE DOMAIN OF THE MEMBRANE PROTEIN TM1634 FROM THERMOTOGA MARITIMA===
-==Overview==
+<!--
-As a part of the Joint Center for Structural Genomics (JCSG) biological targets, the structures of soluble domains of membrane proteins from Thermotoga maritima were pursued. Here, we report the crystal structure of the soluble domain of TM1634, a putative membrane protein of 128 residues (15.1 kDa) and unknown function. The soluble domain of TM1634 is an alpha-helical dimer that contains a single tetratrico peptide repeat (TPR) motif in each monomer where each motif is similar to that found in Tom20. The overall fold, however, is unique and a DALI search does not identify similar folds beyond the 38-residue TPR motif. Two different putative ligand binding sites, in which PEG200 and Co(2+) were located, were identified using crystallography and NMR, respectively.
+The line below this paragraph, {{ABSTRACT_PUBMED_18369189}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18369189 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18369189}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Thermotoga maritima]]
 [[Category: Tpr motif]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:33:55 2008''