1gtt: Difference between revisions

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[[Image:1gtt.gif|left|200px]]
{{Seed}}
[[Image:1gtt.png|left|200px]]


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{{STRUCTURE_1gtt|  PDB=1gtt  |  SCENE=  }}  
{{STRUCTURE_1gtt|  PDB=1gtt  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HPCE'''
===CRYSTAL STRUCTURE OF HPCE===




==Overview==
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The structure of the bifunctional enzyme HpcE (OPET decarboxylase/HHDD isomerase) from Escherichia coli shows that the protein consists of highly similar N and C terminal halves. Sequence matches suggest that this fold is widespread among different species, including man. Many of these homologues are uncharacterized but apparently connected with the metabolism of aromatic compounds. The domain shows similar topology to the C terminal domain of fumarylacetoacetate hydrolase (FAH), a functionally related enzyme, despite lacking significant overall sequence similarity. HpcE is known to catalyze two rather different reactions, and comparisons with FAH allow some tentative conclusions to be drawn about the active sites. Key mutations within the active site apparently allow enzymes with this fold to carry out a variety chemical processes.
The line below this paragraph, {{ABSTRACT_PUBMED_11863436}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11863436 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11863436}}


==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Lyase]]
[[Category: Lyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:00:00 2008''
 
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