1r27
From Proteopedia
(New page: 200px<br /><applet load="1r27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r27, resolution 2.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:1r27.gif|left|200px]]<br /><applet load="1r27" size=" | + | [[Image:1r27.gif|left|200px]]<br /><applet load="1r27" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r27, resolution 2.00Å" /> | caption="1r27, resolution 2.00Å" /> | ||
'''Crystal Structure of NarGH complex'''<br /> | '''Crystal Structure of NarGH complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the catalytic and electron-transfer subunits (NarGH) of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1R27 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MO, F3S, SF4 and MGD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrate_reductase Nitrate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.4 1.7.99.4] Full crystallographic information is available from [http:// | + | 1R27 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MO:'>MO</scene>, <scene name='pdbligand=F3S:'>F3S</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=MGD:'>MGD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrate_reductase Nitrate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.4 1.7.99.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R27 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta barrel; x-ray crystallography]] | [[Category: beta barrel; x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:14 2008'' |
Revision as of 12:46, 21 February 2008
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Crystal Structure of NarGH complex
Overview
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.
About this Structure
1R27 is a Protein complex structure of sequences from Escherichia coli with , , and as ligands. Active as Nitrate reductase, with EC number 1.7.99.4 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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