3ozu: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_3ozu| PDB=3ozu | SCENE= }} | {{STRUCTURE_3ozu| PDB=3ozu | SCENE= }} | ||
===The Crystal Structure of flavohemoglobin from R. eutrophus in complex with miconazole=== | ===The Crystal Structure of flavohemoglobin from R. eutrophus in complex with miconazole=== | ||
{{ABSTRACT_PUBMED_21210640}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/HMP_RALEH HMP_RALEH]] Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.[HAMAP-Rule:MF_01252] In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.[HAMAP-Rule:MF_01252] | |||
-- | |||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021210640</ref><references group="xtra"/><references/> | ||
[[Category: Cupriavidus necator]] | [[Category: Cupriavidus necator]] | ||
[[Category: Nitric oxide dioxygenase]] | [[Category: Nitric oxide dioxygenase]] | ||
| Line 30: | Line 18: | ||
[[Category: Hammi, E El.]] | [[Category: Hammi, E El.]] | ||
[[Category: Warkentin, E.]] | [[Category: Warkentin, E.]] | ||
[[Category: Alpha/beta fold]] | |||
[[Category: Antiparallel beta-barrel]] | |||
[[Category: Fad-]] | |||
[[Category: Globin fold]] | |||
[[Category: Hem-]] | |||
[[Category: Lipid binding protein]] | |||
[[Category: Nad- binding domain]] | |||
Revision as of 11:26, 2 May 2013
The Crystal Structure of flavohemoglobin from R. eutrophus in complex with miconazoleThe Crystal Structure of flavohemoglobin from R. eutrophus in complex with miconazole
Template:ABSTRACT PUBMED 21210640
FunctionFunction
[HMP_RALEH] Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.[HAMAP-Rule:MF_01252] In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.[HAMAP-Rule:MF_01252]
About this StructureAbout this Structure
3ozu is a 1 chain structure with sequence from Cupriavidus necator. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ El Hammi E, Warkentin E, Demmer U, Limam F, Marzouki NM, Ermler U, Baciou L. Structure of Ralstonia eutropha Flavohemoglobin in Complex with Three Antibiotic Azole Compounds. Biochemistry. 2011 Feb 22;50(7):1255-1264. Epub 2011 Jan 20. PMID:21210640 doi:10.1021/bi101650q