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| {{STRUCTURE_1r27| PDB=1r27 | SCENE= }} | | {{STRUCTURE_1r27| PDB=1r27 | SCENE= }} |
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| '''Crystal Structure of NarGH complex'''
| | ===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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14725769}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14725769 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14725769}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta barrel]] | | [[Category: Beta barrel]] |
| [[Category: X-ray crystallography]] | | [[Category: X-ray crystallography]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:59:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:35:16 2008'' |
