1gx3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:09, 13 December 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gx3.gif|left|200px]]
 
-
<!--
+
==M. smegmatis arylamine N-acetyl transferase==
-
The line below this paragraph, containing "STRUCTURE_1gx3", creates the "Structure Box" on the page.
+
<StructureSection load='1gx3' size='340' side='right'caption='[[1gx3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1gx3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GX3 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1gx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx3 OCA], [https://pdbe.org/1gx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gx3 RCSB], [https://www.ebi.ac.uk/pdbsum/1gx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gx3 ProSAT]</span></td></tr>
-
{{STRUCTURE_1gx3| PDB=1gx3 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NAT_MYCSM NAT_MYCSM] Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Substrates include isoniazid, anisidine, and 4-aminoveratrole, and to a much lesser extent, p-aminobenzoic acid.<ref>PMID:12054803</ref> <ref>PMID:9973365</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gx3_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</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=1gx3 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Arylamine N-acetyltransferases which acetylate and inactivate isoniazid, an anti-tubercular drug, are found in mycobacteria including Mycobacterium smegmatis and Mycobacterium tuberculosis. We have solved the structure of arylamine N-acetyltransferase from M. smegmatis at a resolution of 1.7 A as a model for the highly homologous NAT from M. tuberculosis. The fold closely resembles that of NAT from Salmonella typhimurium, with a common catalytic triad and domain structure that is similar to certain cysteine proteases. The detailed geometry of the catalytic triad is typical of enzymes which use primary alcohols or thiols as activated nucleophiles. Thermal mobility and structural variations identify parts of NAT which might undergo conformational changes during catalysis. Sequence conservation among eubacterial NATs is restricted to structural residues of the protein core, as well as the active site and a hinge that connects the first two domains of the NAT structure. The structure of M. smegmatis NAT provides a template for modelling the structure of the M. tuberculosis enzyme and for structure-based ligand design as an approach to designing anti-TB drugs.
-
'''M. SMEGMATIS ARYLAMINE N-ACETYL TRANSFERASE'''
+
The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid.,Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M J Mol Biol. 2002 May 10;318(4):1071-83. PMID:12054803<ref>PMID:12054803</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Arylamine N-acetyltransferases which acetylate and inactivate isoniazid, an anti-tubercular drug, are found in mycobacteria including Mycobacterium smegmatis and Mycobacterium tuberculosis. We have solved the structure of arylamine N-acetyltransferase from M. smegmatis at a resolution of 1.7 A as a model for the highly homologous NAT from M. tuberculosis. The fold closely resembles that of NAT from Salmonella typhimurium, with a common catalytic triad and domain structure that is similar to certain cysteine proteases. The detailed geometry of the catalytic triad is typical of enzymes which use primary alcohols or thiols as activated nucleophiles. Thermal mobility and structural variations identify parts of NAT which might undergo conformational changes during catalysis. Sequence conservation among eubacterial NATs is restricted to structural residues of the protein core, as well as the active site and a hinge that connects the first two domains of the NAT structure. The structure of M. smegmatis NAT provides a template for modelling the structure of the M. tuberculosis enzyme and for structure-based ligand design as an approach to designing anti-TB drugs.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1GX3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX3 OCA].
+
</div>
 +
<div class="pdbe-citations 1gx3" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid., Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M, J Mol Biol. 2002 May 10;318(4):1071-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054803 12054803]
+
*[[Arylamine N-acetyltransferase 3D structures|Arylamine N-acetyltransferase 3D structures]]
-
[[Category: Arylamine N-acetyltransferase]]
+
== References ==
-
[[Category: Mycobacterium smegmatis]]
+
<references/>
-
[[Category: Single protein]]
+
__TOC__
-
[[Category: Kawamura, A.]]
+
</StructureSection>
-
[[Category: Mushtaq, A.]]
+
[[Category: Large Structures]]
-
[[Category: Noble, M.]]
+
[[Category: Mycolicibacterium smegmatis]]
-
[[Category: Sandy, J.]]
+
[[Category: Kawamura A]]
-
[[Category: Sim, E.]]
+
[[Category: Mushtaq A]]
-
[[Category: Sinclair, J.]]
+
[[Category: Noble M]]
-
[[Category: Arylamine n-acetyltransferase]]
+
[[Category: Sandy J]]
-
[[Category: Drug metabolism]]
+
[[Category: Sim E]]
-
[[Category: Isoniazid]]
+
[[Category: Sinclair J]]
-
[[Category: Mycobacteria]]
+
-
[[Category: Nat]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:07:32 2008''
+

Current revision

M. smegmatis arylamine N-acetyl transferase

PDB ID 1gx3

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/1gx3"
Personal tools