1n2a: Difference between revisions

Revision as of 16:07, 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:1n2a.png

Template:STRUCTURE 1n2a

Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active SiteCrystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site

Template:ABSTRACT PUBMED 14635120

About this StructureAbout this Structure

1N2A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli., Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN, Proteins. 2003 Dec 1;53(4):777-82. PMID:14635120

Page seeded by OCA on Tue Jul 29 16:07:35 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1n2a.jpg|left|200px]]
+{{Seed}}
+[[Image:1n2a.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1n2a|  PDB=1n2a  |  SCENE=  }}
-'''Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site'''
+===Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site===
-==Overview==
+<!--
-Multiple sequence alignments of the eight glutathione (GSH) transferase homologues encoded in the genome of Escherichia coli were used to define a consensus sequence for the proteins. The consensus sequence was analyzed in the context of the three-dimensional structure of the gst gene product (EGST) obtained from two different crystal forms of the enzyme. The enzyme consists of two domains. The N-terminal region (domain I) has a thioredoxin-like alpha/beta-fold, while the C-terminal domain (domain II) is all alpha-helical. The majority of the consensus residues (12/17) reside in the N-terminal domain. Fifteen of the 17 residues are involved in hydrophobic core interactions, turns, or electrostatic interactions between the two domains. The results suggest that all of the homologues retain a well-defined group of structural elements both in and between the N-terminal alpha/beta domain and the C-terminal domain. The conservation of two key residues for the recognition motif for the gamma-glutamyl-portion of GSH indicates that the homologues may interact with GSH or GSH analogues such as glutathionylspermidine or alpha-amino acids. The genome context of two of the homologues forms the basis for a hypothesis that the b2989 and yibF gene products are involved in glutathionylspermidine and selenium biochemistry, respectively.
+The line below this paragraph, {{ABSTRACT_PUBMED_14635120}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14635120 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14635120}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Xiao, G.]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:00:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:07:35 2008''