1n2a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1n2a.jpg|left|200px]]
{{Seed}}
[[Image:1n2a.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n2a|  PDB=1n2a  |  SCENE=  }}  
{{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==
==About this Structure==
Line 29: Line 33:
[[Category: Xiao, G.]]
[[Category: Xiao, G.]]
[[Category: Transferase]]
[[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''