1q16
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1q16.gif|left|200px]] | + | [[Image:1q16.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli''' | + | {{Structure |
+ | |PDB= 1q16 |SIZE=350|CAPTION= <scene name='initialview01'>1q16</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MD1:PHOSPHORIC+ACID+4-(2-AMINO-4-OXO-3,4,5,6,-TETRAHYDRO-PTERIDIN-6-YL)-2-HYDROXY-3,4-DIMERCAPTO-BUT-3-EN-YL+ESTER+GUANYLATE+ESTER'>MD1</scene>, <scene name='pdbligand=6MO:MOLYBDENUM(VI)+ION'>6MO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=AGA:(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL+OCTANOATE'>AGA</scene> and <scene name='pdbligand=3PH:1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE'>3PH</scene> | ||
+ | |ACTIVITY= [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] | ||
+ | |GENE= narG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), narH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), narI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1Q16 is a [ | + | 1Q16 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q16 OCA]. |
==Reference== | ==Reference== | ||
- | Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A., Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC, Nat Struct Biol. 2003 Sep;10(9):681-7. Epub 2003 Aug 10. PMID:[http:// | + | Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A., Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC, Nat Struct Biol. 2003 Sep;10(9):681-7. Epub 2003 Aug 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12910261 12910261] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Nitrate reductase]] | [[Category: Nitrate reductase]] | ||
Line 26: | Line 35: | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:31:39 2008'' |
Revision as of 11:31, 20 March 2008
| |||||||
, resolution 1.90Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | , , , , , and | ||||||
Gene: | narG (Escherichia coli), narH (Escherichia coli), narI (Escherichia coli) | ||||||
Activity: | Nitrate reductase, with EC number 1.7.99.4 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of Nitrate Reductase A, NarGHI, from Escherichia coli
Overview
The facultative anaerobe Escherichia coli is able to assemble specific respiratory chains by synthesis of appropriate dehydrogenases and reductases in response to the availability of specific substrates. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A; NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. We present here the crystal structure of NarGHI at a resolution of 1.9 A. The NarGHI structure identifies the number, coordination scheme and environment of the redox-active prosthetic groups, a unique coordination of the molybdenum atom, the first structural evidence for the role of an open bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) (Mo-bisMGD) cofactor in the catalytic mechanism and a novel fold of the membrane anchor subunit. Our findings provide fundamental molecular details for understanding the mechanism of proton-motive force generation by a redox loop.
About this Structure
1Q16 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A., Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC, Nat Struct Biol. 2003 Sep;10(9):681-7. Epub 2003 Aug 10. PMID:12910261
Page seeded by OCA on Thu Mar 20 13:31:39 2008
Categories: Escherichia coli | Nitrate reductase | Protein complex | Bertero, M G. | Strynadka, N C.J. | 3PH | 6MO | AGA | F3S | HEM | MD1 | SF4 | Electron-transfer | Membrane protein