2air

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[[Image:2air.gif|left|200px]]
 
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{{Structure
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==T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme==
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|PDB= 2air |SIZE=350|CAPTION= <scene name='initialview01'>2air</scene>, resolution 2.0&Aring;
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<StructureSection load='2air' size='340' side='right'caption='[[2air]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene> and <scene name='pdbligand=AL0:3-[HYDROXY(NITROSO)AMINO]-L-ALANINE'>AL0</scene>
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<table><tr><td colspan='2'>[[2air]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AIR FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2]
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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&#8491;</td></tr>
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|GENE= pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AL0:3-[HYDROXY(NITROSO)AMINO]-L-ALANINE'>AL0</scene>, <scene name='pdbligand=CP:PHOSPHORIC+ACID+MONO(FORMAMIDE)ESTER'>CP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=2air FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2air OCA], [https://pdbe.org/2air PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2air RCSB], [https://www.ebi.ac.uk/pdbsum/2air PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2air ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI]
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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/ai/2air_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=2air 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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An X-ray diffraction study to 2.0 A resolution shows that this enzyme, ATCase, is in the T-state (the c3 to c3 distance is 45.2 A) when ATCase is bound to carbamyl phosphate (CP) and to L-alanosine (an analogue of aspartate). This result strongly supports the kinetic results that alanosine did not inhibit the carbamylation of aspartate in the normal reaction of native ATCase plus CP and aspartate [Baillon, J., Tauc, P., and Herve, G. (1985) Biochemistry 24, 7182-7187]. The structure further reveals that the phosphate of CP is 4 A away from its known position in the R-state and is in the T-state position of P(i) in a recent study of ATCase complexed with products, phosphate (P(i)) and N-carbamyl-L-aspartate [Huang, J., and Lipscomb, W. N. (2004) Biochemistry 43, 6422-6426]. Moreover, the alanosine position in this T-state is somewhat displaced from that expected for its analogue, aspartate, from the R-state position. The relations of these structural aspects to the kinetics are presented.
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'''T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme'''
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T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme.,Huang J, Lipscomb WN Biochemistry. 2006 Jan 17;45(2):346-52. PMID:16401065<ref>PMID:16401065</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 2air" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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An X-ray diffraction study to 2.0 A resolution shows that this enzyme, ATCase, is in the T-state (the c3 to c3 distance is 45.2 A) when ATCase is bound to carbamyl phosphate (CP) and to L-alanosine (an analogue of aspartate). This result strongly supports the kinetic results that alanosine did not inhibit the carbamylation of aspartate in the normal reaction of native ATCase plus CP and aspartate [Baillon, J., Tauc, P., and Herve, G. (1985) Biochemistry 24, 7182-7187]. The structure further reveals that the phosphate of CP is 4 A away from its known position in the R-state and is in the T-state position of P(i) in a recent study of ATCase complexed with products, phosphate (P(i)) and N-carbamyl-L-aspartate [Huang, J., and Lipscomb, W. N. (2004) Biochemistry 43, 6422-6426]. Moreover, the alanosine position in this T-state is somewhat displaced from that expected for its analogue, aspartate, from the R-state position. The relations of these structural aspects to the kinetics are presented.
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*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2AIR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIR OCA].
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__TOC__
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</StructureSection>
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==Reference==
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T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme., Huang J, Lipscomb WN, Biochemistry. 2006 Jan 17;45(2):346-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16401065 16401065]
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[[Category: Aspartate carbamoyltransferase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Huang, J.]]
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[[Category: Huang J]]
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[[Category: Lipscomb, W N.]]
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[[Category: Lipscomb WN]]
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[[Category: AL0]]
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[[Category: CP]]
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[[Category: ZN]]
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[[Category: alanosine]]
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[[Category: aspartate transcarbamylase]]
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[[Category: carbamyl phosphate]]
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[[Category: t-state]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:50:10 2008''
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Current revision

T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme

PDB ID 2air

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