1kfy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1kfy.jpg|left|200px]]
{{Seed}}
[[Image:1kfy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kfy|  PDB=1kfy  |  SCENE=  }}  
{{STRUCTURE_1kfy|  PDB=1kfy  |  SCENE=  }}  


'''QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'''
===QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL===




==Overview==
<!--  
The quinol-fumarate reductase (QFR) respiratory complex of Escherichia coli is a four-subunit integral-membrane complex that catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor. The membrane-soluble redox-active molecule menaquinol (MQH(2)) transfers electrons to QFR by binding directly to the membrane-spanning region. The crystal structure of QFR contains two quinone species, presumably MQH(2), bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed Q(P) and Q(D), indicating their positions proximal (Q(P)) or distal (Q(D)) to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. It has not been established whether both of these sites are mechanistically significant. Co-crystallization studies of the E. coli QFR with the known quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH(2) at the Q(P) site. In the structures with the inhibitor bound at Q(P), no density is observed at Q(D), which suggests that the occupancy of this site can vary and argues against a structurally obligatory role for quinol binding to Q(D). A comparison of the Q(P) site of the E. coli enzyme with quinone-binding sites in other respiratory enzymes shows that an acidic residue is structurally conserved. This acidic residue, Glu-C29, in the E. coli enzyme may act as a proton shuttle from the quinol during enzyme turnover.
The line below this paragraph, {{ABSTRACT_PUBMED_11850430}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11850430 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11850430}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Respiration]]
[[Category: Respiration]]
[[Category: Succinate dehydrogenase]]
[[Category: Succinate dehydrogenase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:42:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:17:18 2008''

Revision as of 07:17, 2 July 2008

File:1kfy.png

Template:STRUCTURE 1kfy

QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL

Template:ABSTRACT PUBMED 11850430

About this Structure

1KFY is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site., Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC, J Biol Chem. 2002 May 3;277(18):16124-30. Epub 2002 Feb 15. PMID:11850430

Page seeded by OCA on Wed Jul 2 10:17:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1kfy&oldid=620660"