3tw7

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[[Image:3tw7.png|left|200px]]
 
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==Structure of Rhizobium etli pyruvate carboxylase T882A crystallized without acetyl coenzyme-A==
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The line below this paragraph, containing "STRUCTURE_3tw7", creates the "Structure Box" on the page.
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<StructureSection load='3tw7' size='340' side='right'caption='[[3tw7]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3tw7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_etli_CFN_42 Rhizobium etli CFN 42]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW7 FirstGlance]. <br>
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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]] 3.1&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3tw7| PDB=3tw7 | 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=3tw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw7 OCA], [https://pdbe.org/3tw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q2K340_RHIEC Q2K340_RHIEC] Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (By similarity).[PIRNR:PIRNR001594]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate, an important anaplerotic reaction in mammalian tissues. To effect catalysis, the tethered biotin of PC must gain access to active sites in both the biotin carboxylase domain and the carboxyl transferase domain. Previous studies have demonstrated that a mutation of threonine 882 to alanine in PC from Rhizobium etli renders the carboxyl transferase domain inactive and favors the positioning of biotin in the biotin carboxylase domain. We report the 2.4 A resolution X-ray crystal structure of the Rhizobium etli PC T882A mutant which reveals the first high-resolution description of the domain interaction between the biotin carboxyl carrier protein domain and the biotin carboxylase domain. The overall quaternary arrangement of Rhizobium etli PC remains highly asymmetrical and is independent of the presence of allosteric activator. While biotin is observed in the biotin carboxylase domain, its access to the active site is precluded by the interaction between Arg353 and Glu248, revealing a mechanism for regulating carboxybiotin access to the BC domain active site. The binding location for the biotin carboxyl carrier protein domain demonstrates that tethered biotin cannot bind in the biotin carboxylase domain active site in the same orientation as free biotin, helping to explain the difference in catalysis observed between tethered biotin and free biotin substrates in biotin carboxylase enzymes. Electron density located in the biotin carboxylase domain active site is assigned to phosphonoacetate, offering a probable location for the putative carboxyphosphate intermediate formed during biotin carboxylation. The insights gained from the T882A Rhizobium etli PC crystal structure provide a new series of catalytic snapshots in PC and offer a revised perspective on catalysis in the biotin-dependent enzyme family.
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===Structure of Rhizobium etli pyruvate carboxylase T882A crystallized without acetyl coenzyme-A===
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Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli.,Lietzan AD, Menefee AL, Zeczycki TN, Kumar S, Attwood PV, Wallace JC, Cleland WW, St Maurice M Biochemistry. 2011 Oct 18. PMID:21958016<ref>PMID:21958016</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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</div>
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<div class="pdbe-citations 3tw7" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21958016 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21958016}}
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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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[[3tw7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizobium_etli Rhizobium etli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW7 OCA].
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[[Category: Rhizobium etli CFN 42]]
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[[Category: Kumar S]]
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==Reference==
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[[Category: Lietzan AD]]
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<ref group="xtra">PMID:021958016</ref><references group="xtra"/>
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[[Category: St Maurice M]]
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[[Category: Pyruvate carboxylase]]
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[[Category: Rhizobium etli]]
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[[Category: Kumar, S.]]
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[[Category: Lietzan, A D.]]
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[[Category: Maurice, M St.]]
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[[Category: Biotin carboxylase]]
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[[Category: Ligase]]
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Current revision

Structure of Rhizobium etli pyruvate carboxylase T882A crystallized without acetyl coenzyme-A

PDB ID 3tw7

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