2nap: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2nap.gif|left|200px]]
{{Seed}}
[[Image:2nap.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nap|  PDB=2nap  |  SCENE=  }}  
{{STRUCTURE_2nap|  PDB=2nap  |  SCENE=  }}  


'''DISSIMILATORY NITRATE REDUCTASE (NAP) FROM DESULFOVIBRIO DESULFURICANS'''
===DISSIMILATORY NITRATE REDUCTASE (NAP) FROM DESULFOVIBRIO DESULFURICANS===




==Overview==
<!--
BACKGROUND: The periplasmic nitrate reductase (NAP) from the sulphate reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is induced by growth on nitrate and catalyses the reduction of nitrate to nitrite for respiration. NAP is a molybdenum-containing enzyme with one bis-molybdopterin guanine dinucleotide (MGD) cofactor and one [4Fe-4S] cluster in a single polypeptide chain of 723 amino acid residues. To date, there is no crystal structure of a nitrate reductase. RESULTS: The first crystal structure of a dissimilatory (respiratory) nitrate reductase was determined at 1.9 A resolution by multiwavelength anomalous diffraction (MAD) methods. The structure is folded into four domains with an alpha/beta-type topology and all four domains are involved in cofactor binding. The [4Fe-4S] centre is located near the periphery of the molecule, whereas the MGD cofactor extends across the interior of the molecule interacting with residues from all four domains. The molybdenum atom is located at the bottom of a 15 A deep crevice, and is positioned 12 A from the [4Fe-4S] cluster. The structure of NAP reveals the details of the catalytic molybdenum site, which is coordinated to two MGD cofactors, Cys140, and a water/hydroxo ligand. A facile electron-transfer pathway through bonds connects the molybdenum and the [4Fe-4S] cluster. CONCLUSIONS: The polypeptide fold of NAP and the arrangement of the cofactors is related to that of Escherichia coli formate dehydrogenase (FDH) and distantly resembles dimethylsulphoxide reductase. The close structural homology of NAP and FDH shows how small changes in the vicinity of the molybdenum catalytic site are sufficient for the substrate specificity.
The line below this paragraph, {{ABSTRACT_PUBMED_10368307}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10368307 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10368307}}


==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Multiwavelength anomalous diffraction]]
[[Category: Multiwavelength anomalous diffraction]]
[[Category: Nitrogenous acceptor]]
[[Category: Nitrogenous acceptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:35:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:59:35 2008''

Revision as of 12:59, 27 July 2008

File:2nap.png

Template:STRUCTURE 2nap

DISSIMILATORY NITRATE REDUCTASE (NAP) FROM DESULFOVIBRIO DESULFURICANS

Template:ABSTRACT PUBMED 10368307

About this Structure

2NAP is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.

Reference

Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods., Dias JM, Than ME, Humm A, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Calvete J, Caldeira J, Carneiro C, Moura JJ, Moura I, Romao MJ, Structure. 1999 Jan 15;7(1):65-79. PMID:10368307

Page seeded by OCA on Sun Jul 27 15:59:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2nap&oldid=654683"