3it6

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{{Seed}}
 
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[[Image:3it6.png|left|200px]]
 
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==The Crystal Structure of Ornithine Acetyltransferase complexed with Ornithine from Mycobacterium tuberculosis (Rv1653) at 2.4 A==
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The line below this paragraph, containing "STRUCTURE_3it6", creates the "Structure Box" on the page.
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<StructureSection load='3it6' size='340' side='right'caption='[[3it6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3it6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IT6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></td></tr>
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{{STRUCTURE_3it6| PDB=3it6 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3it6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3it6 OCA], [https://pdbe.org/3it6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3it6 RCSB], [https://www.ebi.ac.uk/pdbsum/3it6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3it6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARGJ_MYCTU ARGJ_MYCTU] Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate (By similarity).[HAMAP-Rule:MF_01106]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/3it6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3it6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mycobacterium tuberculosis ornithine acetyltransferase (Mtb OAT; E.C. 2.3.1.35) is a key enzyme of the acetyl recycling pathway during arginine biosynthesis. It reversibly catalyzes the transfer of the acetyl group from N-acetylornithine (NAORN) to L-glutamate. Mtb OAT is a member of the N-terminal nucleophile fold family of enzymes. The crystal structures of Mtb OAT in native form and in its complex with ornithine (ORN) have been determined at 1.7 and 2.4 A resolutions, respectively. ORN is a competitive inhibitor of this enzyme against L-glutamate as substrate. Although the acyl-enzyme complex of Streptomyces clavuligerus ornithine acetyltransferase has been determined, ours is the first crystal structure to be reported of an ornithine acetyltransferase in complex with an inhibitor. ORN binding does not alter the structure of Mtb OAT globally. However, its presence stabilizes the three C-terminal residues that are disordered and not observed in the native structure. Also, stabilization of the C-terminal residues by ORN reduces the size of the active-site pocket volume in the structure of the ORN complex. The interactions of ORN and the protein residues of Mtb OAT unambiguously delineate the active-site residues of this enzyme in Mtb. Moreover, modeling studies carried out with NAORN based on the structure of the ORN-Mtb OAT complex reveal important interactions of the carbonyl oxygen of the acetyl group of NAORN with the main-chain nitrogen atom of Gly128 and with the side-chain oxygen of Thr127. These interactions likely help in the stabilization of oxyanion formation during enzymatic reaction and also will polarize the carbonyl carbon-oxygen bond, thereby enabling the side-chain atom O(gamma 1) of Thr200 to launch a nucleophilic attack on the carbonyl-carbon atom of the acetyl group of NAORN.
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===The Crystal Structure of Ornithine Acetyltransferase complexed with Ornithine from Mycobacterium tuberculosis (Rv1653) at 2.4 A===
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The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor.,Sankaranarayanan R, Cherney MM, Garen C, Garen G, Niu C, Yuan M, James MN J Mol Biol. 2010 Apr 9;397(4):979-90. Epub 2010 Feb 22. PMID:20184895<ref>PMID:20184895</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_20184895}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3it6" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20184895 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20184895}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3IT6 is a 4 chains structure with sequences 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=3IT6 OCA].
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==Reference==
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<ref group="xtra">PMID:20184895</ref><references group="xtra"/>
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[[Category: Glutamate N-acetyltransferase]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Cherney, M M.]]
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[[Category: Cherney MM]]
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[[Category: Garen, C.]]
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[[Category: Garen C]]
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[[Category: Garen, G.]]
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[[Category: Garen G]]
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[[Category: James, M N.]]
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[[Category: James MN]]
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[[Category: Sankaranarayanan, R.]]
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[[Category: Sankaranarayanan R]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Yuan M]]
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[[Category: Yuan, M.]]
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[[Category: Acyltransferase]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Arginine biosynthesis]]
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[[Category: Cytoplasm]]
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[[Category: Multifunctional enzyme]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Ornithine acetyltransferase]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 09:12:58 2010''
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Current revision

The Crystal Structure of Ornithine Acetyltransferase complexed with Ornithine from Mycobacterium tuberculosis (Rv1653) at 2.4 A

PDB ID 3it6

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