1r27

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[[Image:1r27.gif|left|200px]]
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{{STRUCTURE_1r27| PDB=1r27 | SCENE= }}
{{STRUCTURE_1r27| PDB=1r27 | SCENE= }}
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'''Crystal Structure of NarGH complex'''
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===Crystal Structure of NarGH complex===
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==Overview==
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The structure of the catalytic and electron-transfer subunits (NarGH) of the integral membrane protein, respiratory nitrate reductase (Nar) has been determined to 2.0 A resolution revealing the molecular architecture of this Mo-bisMGD (molybdopterin-guanine-dinucleotide) containing enzyme which includes a previously undetected FeS cluster. Nar, together with the related enzyme formate dehydrogenase (Fdh-N), is a key enzyme in the generation of proton motive force across the membrane in Escherichia coli nitrate respiration. A comparative study revealed that Nar and Fdh-N employ different approaches for acquiring substrate, reflecting different catalytic mechanisms. Nar uses a very narrow and nonpolar substrate-conducting cavity with a nonspecific substrate binding site, whereas Fdh-N accommodates a wider, positively charged substrate-conducting cavity with a more specific substrate binding site. The Nar structure also demonstrates the first example of an Asp side chain acting as a Mo ligand providing a structural basis for the classification of Mo-bisMGD enzymes.
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{{ABSTRACT_PUBMED_14725769}}
==About this Structure==
==About this Structure==
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[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:35:16 2008''

Revision as of 20:35, 27 July 2008

Image:1r27.png

Template:STRUCTURE 1r27

Crystal Structure of NarGH complex

Template:ABSTRACT PUBMED 14725769

About this Structure

1R27 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes., Jormakka M, Richardson D, Byrne B, Iwata S, Structure. 2004 Jan;12(1):95-104. PMID:14725769

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