1gu9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1gu9.gif|left|200px]]
{{Seed}}
[[Image:1gu9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gu9|  PDB=1gu9  |  SCENE=  }}  
{{STRUCTURE_1gu9|  PDB=1gu9  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALKYLPEROXIDASE AHPD'''
===CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALKYLPEROXIDASE AHPD===




==Overview==
<!--
The resistance of Mycobacterium tuberculosis to isoniazid is commonly linked to inactivation of a catalase-peroxidase, KatG, that converts isoniazid to its biologically active form. Loss of KatG is associated with elevated expression of the alkylhydroperoxidases AhpC and AhpD. AhpD has no sequence identity with AhpC or other proteins but has alkylhydroperoxidase activity and possibly additional physiological activities. The alkylhydroperoxidase activity, in the absence of KatG, provides an important antioxidant defense. We have determined the M. tuberculosis AhpD structure to a resolution of 1.9 A. The protein is a trimer in a symmetrical cloverleaf arrangement. Each subunit exhibits a new all-helical protein fold in which the two catalytic sulfhydryl groups, Cys-130 and Cys-133, are located near a central cavity in the trimer. The structure supports a mechanism for the alkylhydroperoxidase activity in which Cys-133 is deprotonated by a distant glutamic acid via the relay action of His-137 and a water molecule. The cysteine then reacts with the peroxide to give a sulfenic acid that subsequently forms a disulfide bond with Cys-130. The crystal structure of AhpD identifies a new protein fold relevant to members of this protein family in other organisms. The structural details constitute a potential platform for the design of inhibitors of potential utility as antitubercular agents and suggest that AhpD may have disulfide exchange properties of importance in other areas of M. tuberculosis biology.
The line below this paragraph, {{ABSTRACT_PUBMED_11914371}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11914371 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11914371}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alkylhydroperoxidase]]
[[Category: Alkylhydroperoxidase]]
[[Category: Tuberculosis]]
[[Category: Tuberculosis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:00:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:05:19 2008''

Revision as of 03:05, 1 July 2008

File:1gu9.png

Template:STRUCTURE 1gu9

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALKYLPEROXIDASE AHPD

Template:ABSTRACT PUBMED 11914371

About this Structure

1GU9 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design., Nunn CM, Djordjevic S, Hillas PJ, Nishida CR, Ortiz de Montellano PR, J Biol Chem. 2002 May 31;277(22):20033-40. Epub 2002 Mar 25. PMID:11914371

Page seeded by OCA on Tue Jul 1 06:05:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gu9&oldid=603939"