3bg3

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(New page: 200px<br /><applet load="3bg3" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bg3, resolution 2.80&Aring;" /> '''Crystal Structure of...)
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[[Image:3bg3.jpg|left|200px]]<br /><applet load="3bg3" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bg3, resolution 2.80&Aring;" />
 
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'''Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)'''<br />
 
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==About this Structure==
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==Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)==
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3BG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=PYR:'>PYR</scene> and <scene name='pdbligand=BTI:'>BTI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] Known structural/functional Sites: <scene name='pdbsite=AC1:Mn+Binding+Site+For+Residue+A+2001'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Residue+B+2001'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+C+2001'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Residue+D+2001'>AC4</scene>, <scene name='pdbsite=AC5:Pyr+Binding+Site+For+Residue+A+2000'>AC5</scene>, <scene name='pdbsite=AC6:Bti+Binding+Site+For+Residue+A+2100'>AC6</scene>, <scene name='pdbsite=AC7:Pyr+Binding+Site+For+Residue+B+2000'>AC7</scene>, <scene name='pdbsite=AC8:Pyr+Binding+Site+For+Residue+C+2000'>AC8</scene> and <scene name='pdbsite=AC9:Pyr+Binding+Site+For+Residue+D+2000'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BG3 OCA].
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<StructureSection load='3bg3' size='340' side='right'caption='[[3bg3]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Pyruvate carboxylase]]
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<table><tr><td colspan='2'>[[3bg3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BG3 FirstGlance]. <br>
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[[Category: Single protein]]
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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]] 2.8&#8491;</td></tr>
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[[Category: Tong, L.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTI:5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL'>BTI</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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[[Category: Xiang, S.]]
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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=3bg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bg3 OCA], [https://pdbe.org/3bg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bg3 RCSB], [https://www.ebi.ac.uk/pdbsum/3bg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bg3 ProSAT]</span></td></tr>
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[[Category: BTI]]
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</table>
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[[Category: MN]]
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== Disease ==
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[[Category: PYR]]
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[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Defects in PC are the cause of pyruvate carboxylase deficiency (PC deficiency) [MIM:[https://omim.org/entry/266150 266150]. PC deficiency leads to lactic acidosis, mental retardation and death. It occurs in three forms: mild or type A, severe neonatal or type B, and a very mild lacticacidemia.
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[[Category: atp-binding]]
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== Function ==
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[[Category: biotin]]
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[https://www.uniprot.org/uniprot/PYC_HUMAN PYC_HUMAN] Pyruvate carboxylase 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. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
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[[Category: disease mutation]]
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== Evolutionary Conservation ==
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[[Category: gluconeogenesis]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: ligase]]
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Check<jmol>
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[[Category: lipid synthesis]]
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<jmolCheckbox>
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[[Category: manganese]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bg3_consurf.spt"</scriptWhenChecked>
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[[Category: mitochondrion]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: multifunctional enzyme]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: nucleotide-binding]]
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</jmolCheckbox>
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[[Category: phosphoprotein]]
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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=3bg3 ConSurf].
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[[Category: tim barrel]]
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<div style="clear:both"></div>
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[[Category: transit peptide]]
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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 biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes. PC contains the biotin carboxylase (BC), carboxyltransferase (CT) and biotin-carboxyl carrier protein (BCCP) domains. We report here the crystal structures at 2.8-A resolution of full-length PC from Staphylococcus aureus and the C-terminal region (missing only the BC domain) of human PC. A conserved tetrameric association is observed for both enzymes, and our structural and mutagenesis studies reveal a previously uncharacterized domain, the PC tetramerization (PT) domain, which is important for oligomerization. A BCCP domain is located in the active site of the CT domain, providing the first molecular insights into how biotin participates in the carboxyltransfer reaction. There are dramatic differences in domain positions in the monomer and the organization of the tetramer between these enzymes and the PC from Rhizobium etli.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:59:47 2008''
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Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.,Xiang S, Tong L Nat Struct Mol Biol. 2008 Mar;15(3):295-302. Epub 2008 Feb 24. PMID:18297087<ref>PMID:18297087</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 3bg3" 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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Tong L]]
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[[Category: Xiang S]]

Current revision

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)

PDB ID 3bg3

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