1m6v

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(New page: 200px<br /><applet load="1m6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6v, resolution 2.10&Aring;" /> '''Crystal Structure of...)
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[[Image:1m6v.jpg|left|200px]]<br /><applet load="1m6v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m6v, resolution 2.10&Aring;" />
 
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'''Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase'''<br />
 
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==Overview==
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==Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase==
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Carbamoyl-phosphate synthetase catalyzes the production of carbamoyl, phosphate through a reaction mechanism requiring one molecule of, bicarbonate, two molecules of MgATP, and one molecule of glutamine. The, enzyme from Escherichia coli is composed of two polypeptide chains. The, smaller of these belongs to the Class I amidotransferase superfamily and, contains all of the necessary amino acid side chains required for the, hydrolysis of glutamine to glutamate and ammonia. Two homologous domains, from the larger subunit adopt conformations that are characteristic for, members of the ATP-grasp superfamily. Each of these ATP-grasp domains, contains an active site responsible for binding one molecule of MgATP., High resolution x-ray crystallographic analyses have shown that, remarkably, the three active sites in the E. coli enzyme are connected by, a molecular tunnel of approximately 100 A in total length. Here we, describe the high resolution x-ray crystallographic structure of the G359F, (small subunit) mutant protein of carbamoyl phosphate synthetase. This, residue was initially targeted for study because it resides within the, interior wall of the molecular tunnel leading from the active site of the, small subunit to the first active site of the large subunit. It was, anticipated that a mutation to the larger residue would "clog" the ammonia, tunnel and impede the delivery of ammonia from its site of production to, the site of utilization. In fact, the G359F substitution resulted in a, complete change in the conformation of the loop delineated by Glu-355 to, Ala-364, thereby providing an "escape" route for the ammonia intermediate, directly to the bulk solvent. The substitution also effected the, disposition of several key catalytic amino acid side chains in the small, subunit active site.
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<StructureSection load='1m6v' size='340' side='right'caption='[[1m6v]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m6v]] is a 8 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=1M6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M6V 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]] 2.1&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NET:TETRAETHYLAMMONIUM+ION'>NET</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=1m6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6v OCA], [https://pdbe.org/1m6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6v RCSB], [https://www.ebi.ac.uk/pdbsum/1m6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARB_ECOLI CARB_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/m6/1m6v_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=1m6v ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, K, CL, PO4, ADP, ORN and NET as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbamoyl-phosphate_synthase_(glutamine-hydrolyzing) Carbamoyl-phosphate synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.5 6.3.5.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6V OCA].
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*[[Carbamoyl phosphate synthetase 3D structures|Carbamoyl phosphate synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia., Thoden JB, Huang X, Raushel FM, Holden HM, J Biol Chem. 2002 Oct 18;277(42):39722-7. Epub 2002 Jul 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12130656 12130656]
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[[Category: Carbamoyl-phosphate synthase (glutamine-hydrolyzing)]]
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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: Holden, H.M.]]
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[[Category: Holden HM]]
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[[Category: Huang, X.]]
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[[Category: Huang X]]
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[[Category: Raushel, F.M.]]
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[[Category: Raushel FM]]
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[[Category: Thoden, J.B.]]
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[[Category: Thoden JB]]
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[[Category: ADP]]
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[[Category: CL]]
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[[Category: K]]
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[[Category: MN]]
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[[Category: NET]]
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[[Category: ORN]]
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[[Category: PO4]]
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[[Category: substrate channeling]]
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[[Category: tunnel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:11:32 2007''
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Current revision

Crystal Structure of the G359F (small subunit) Point Mutant of Carbamoyl Phosphate Synthetase

PDB ID 1m6v

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