2y79: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2y79.png|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2y79", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2y79|  PDB=2y79  |  SCENE=  }}  
{{STRUCTURE_2y79|  PDB=2y79  |  SCENE=  }}  
===STRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSS===
===STRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSS===
{{ABSTRACT_PUBMED_21536032}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/DEVS_MYCTU DEVS_MYCTU]] Member of the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. May act as a redox sensor (rather than a direct hypoxia sensor); the normal (aerobic growth) state is the Fe(3+) form, while the reduced (anaerobic growth) Fe(2+) form is probably active for phosphate transfer. It is probably reduced by flavin nucleotides such as FMN and FAD. May be the primary sensor for CO. Donates a phosphate group to DevR (DosR).<ref>PMID:15033981</ref> <ref>PMID:18474359</ref> <ref>PMID:18400743</ref>
The line below this paragraph, {{ABSTRACT_PUBMED_21536032}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 21536032 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_21536032}}


==About this Structure==
==About this Structure==
Line 22: Line 10:


==Reference==
==Reference==
<ref group="xtra">PMID:021536032</ref><references group="xtra"/>
<ref group="xtra">PMID:021536032</ref><references group="xtra"/><references/>
[[Category: Histidine kinase]]
[[Category: Histidine kinase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]

Revision as of 14:48, 24 April 2013

Template:STRUCTURE 2y79

STRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSSSTRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSS

Template:ABSTRACT PUBMED 21536032

FunctionFunction

[DEVS_MYCTU] Member of the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. May act as a redox sensor (rather than a direct hypoxia sensor); the normal (aerobic growth) state is the Fe(3+) form, while the reduced (anaerobic growth) Fe(2+) form is probably active for phosphate transfer. It is probably reduced by flavin nucleotides such as FMN and FAD. May be the primary sensor for CO. Donates a phosphate group to DevR (DosR).[1] [2] [3]

About this StructureAbout this Structure

2y79 is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Cho HY, Cho HJ, Kim MH, Kang BS. Blockage of the channel to heme by the E87 side chain in the GAF domain of Mycobacterium tuberculosis DosS confers the unique sensitivity of DosS to oxygen. FEBS Lett. 2011 Jun 23;585(12):1873-8. Epub 2011 Apr 27. PMID:21536032 doi:10.1016/j.febslet.2011.04.050
  1. Roberts DM, Liao RP, Wisedchaisri G, Hol WG, Sherman DR. Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J Biol Chem. 2004 May 28;279(22):23082-7. Epub 2004 Mar 19. PMID:15033981 doi:10.1074/jbc.M401230200
  2. Shiloh MU, Manzanillo P, Cox JS. Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe. 2008 May 15;3(5):323-30. doi: 10.1016/j.chom.2008.03.007. PMID:18474359 doi:10.1016/j.chom.2008.03.007
  3. Kumar A, Deshane JS, Crossman DK, Bolisetty S, Yan BS, Kramnik I, Agarwal A, Steyn AJ. Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon. J Biol Chem. 2008 Jun 27;283(26):18032-9. doi: 10.1074/jbc.M802274200. Epub 2008 , Apr 9. PMID:18400743 doi:10.1074/jbc.M802274200

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA