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1g5t

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(New page: 200px<br /><applet load="1g5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5t, resolution 1.8&Aring;" /> '''THE THREE-DIMENSIONAL...)
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[[Image:1g5t.jpg|left|200px]]<br /><applet load="1g5t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g5t, resolution 1.8&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF ATP:CORRINOID ADENOSYLTRANSFERASE FROM SALMONELLA TYPHIMURIUM. APO-ATP FORM'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF ATP:CORRINOID ADENOSYLTRANSFERASE FROM SALMONELLA TYPHIMURIUM. APO-ATP FORM==
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In Salmonella typhimurium, formation of the cobalt-carbon bond in the, biosynthetic pathway for adenosylcobalamin is catalyzed by the product of, the cobA gene which encodes a protein of 196 amino acid residues. This, enzyme is an ATP:co(I)rrinoid adenosyltransferase which transfers an, adenosyl moiety from MgATP to a broad range of co(I)rrinoid substrates, that are believed to include cobinamide, its precursor cobyric acid and, probably others as yet unidentified, and hydroxocobalamin. Three X-ray, structures of CobA are reported here: its substrate-free form, a complex, of CobA with MgATP, and a ternary complex of CobA with MgATP and, hydroxycobalamin to 2.1, 1.8, and 2.1 A resolution, respectively. These, structures show that the enzyme is a homodimer. In the apo structure, the, polypeptide chain extends from Arg(28) to Lys(181) and consists of an, alpha/beta structure built from a six-stranded parallel beta-sheet with, strand order 324516. The topology of this fold is very similar to that, seen in RecA protein, helicase domain, F(1)ATPase, and adenosylcobinamide, kinase/adenosylcobinamide guanylyltransferase where a P-loop is located at, the end of the first strand. Strikingly, the nucleotide in the MgATP.CobA, complex binds to the P-loop of CobA in the opposite orientation compared, to all the other nucleotide hydrolases. That is, the gamma-phosphate binds, at the location normally occupied by the alpha-phosphate. The unusual, orientation of the nucleotide arises because this enzyme transfers an, adenosyl group rather than the gamma-phosphate. In the ternary complex, the binding site for hydroxycobalamin is located in a shallow bowl-shaped, depression at the C-terminal end of the beta-sheet of one subunit;, however, the active site is capped by the N-terminal helix from the, symmetry-related subunit that now extends from Gln(7) to Ala(24). The, lower ligand of cobalamin is well-ordered and interacts mostly with the, N-terminal helix of the symmetry-related subunit. Interestingly, there are, few interactions between the protein and the polar side chains of the, corrin ring which accounts for the broad specificity of this enzyme. The, corrin ring is oriented such that the cobalt atom is located approximately, 6.1 A from C5' of the ribose and is beyond the range of nucleophilic, attack. This suggests that a conformational change occurs in the ternary, complex when Co(III) is reduced to Co(I).
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<StructureSection load='1g5t' size='340' side='right'caption='[[1g5t]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1g5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5T FirstGlance]. <br>
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1G5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cob(I)yrinic_acid_a,c-diamide_adenosyltransferase Cob(I)yrinic acid a,c-diamide adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.17 2.5.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G5T OCA].
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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]] 1.8&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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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=1g5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5t OCA], [https://pdbe.org/1g5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5t RCSB], [https://www.ebi.ac.uk/pdbsum/1g5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5t ProSAT]</span></td></tr>
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Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP., Bauer CB, Fonseca MV, Holden HM, Thoden JB, Thompson TB, Escalante-Semerena JC, Rayment I, Biochemistry. 2001 Jan 16;40(2):361-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11148030 11148030]
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</table>
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[[Category: Cob(I)yrinic acid a,c-diamide adenosyltransferase]]
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== Function ==
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[[Category: Salmonella typhimurium]]
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[https://www.uniprot.org/uniprot/BTUR_SALTY BTUR_SALTY] Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Bauer, C.B.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Escalante-Semerena, J.C.]]
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Check<jmol>
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[[Category: Rayment, I.]]
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<jmolCheckbox>
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[[Category: ATP]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/1g5t_consurf.spt"</scriptWhenChecked>
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[[Category: MG]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: cobalamin biosynthesis]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: p-loop protein]]
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</jmolCheckbox>
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[[Category: reca fold]]
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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=1g5t ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:43:56 2007''
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Bauer CB]]
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[[Category: Escalante-Semerena JC]]
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[[Category: Rayment I]]

Current revision

THE THREE-DIMENSIONAL STRUCTURE OF ATP:CORRINOID ADENOSYLTRANSFERASE FROM SALMONELLA TYPHIMURIUM. APO-ATP FORM

PDB ID 1g5t

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