This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gu9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:24, 27 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gu9.gif|left|200px]]
 
-
{{Structure
+
==Crystal Structure of Mycobacterium tuberculosis Alkylperoxidase AhpD==
-
|PDB= 1gu9 |SIZE=350|CAPTION= <scene name='initialview01'>1gu9</scene>, resolution 1.9&Aring;
+
<StructureSection load='1gu9' size='340' side='right'caption='[[1gu9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1gu9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GU9 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
}}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu9 OCA], [https://pdbe.org/1gu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu9 ProSAT]</span></td></tr>
-
 
+
</table>
-
'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ALKYLPEROXIDASE AHPD'''
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
==Overview==
+
<jmolCheckbox>
-
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.
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1gu9_consurf.spt"</scriptWhenChecked>
-
 
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
==About this Structure==
+
<text>to colour the structure by Evolutionary Conservation</text>
-
1GU9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU9 OCA].
+
</jmolCheckbox>
-
 
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gu9 ConSurf].
-
==Reference==
+
<div style="clear:both"></div>
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/11914371 11914371]
+
__TOC__
-
[[Category: Mycobacterium tuberculosis]]
+
</StructureSection>
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Djordjevic, S.]]
+
[[Category: Mycobacterium tuberculosis H37Rv]]
-
[[Category: Hillas, P J.]]
+
[[Category: Djordjevic S]]
-
[[Category: Montellano, P R.O De.]]
+
[[Category: Hillas PJ]]
-
[[Category: Nishida, C.]]
+
[[Category: Nishida C]]
-
[[Category: Nunn, C M.]]
+
[[Category: Nunn CM]]
-
[[Category: alkylhydroperoxidase]]
+
[[Category: Ortiz de Montellano PR]]
-
[[Category: tuberculosis]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:02 2008''
+

Current revision

Crystal Structure of Mycobacterium tuberculosis Alkylperoxidase AhpD

PDB ID 1gu9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gu9"
Personal tools