1yk9

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(New page: 200px<br /><applet load="1yk9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yk9, resolution 2.70&Aring;" /> '''Crystal structure of...)
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[[Image:1yk9.gif|left|200px]]<br /><applet load="1yk9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yk9, resolution 2.70&Aring;" />
 
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'''Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c'''<br />
 
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==Overview==
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==Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c==
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The Rv1625c Class III adenylyl cyclase from Mycobacterium tuberculosis is, a homodimeric enzyme with two catalytic centers at the dimer interface, and shows sequence similarity with the mammalian adenylyl and guanylyl, cyclases. Mutation of the substrate-specifying residues in the catalytic, domain of Rv1625c, either independently or together, to those present in, guanylyl cyclases not only failed to confer guanylyl cyclase activity to, the protein, but also severely abrogated the adenylyl cyclase activity of, the enzyme. Biochemical analysis revealed alterations in the behavior of, the mutants on ion-exchange chromatography, indicating differences in the, surface-exposed charge upon mutation of substrate-specifying residues. The, mutant proteins showed alterations in oligomeric status as compared to the, wild-type enzyme, and differing abilities to heterodimerize with the, wild-type protein. The crystal structure of a mutant has been solved to a, resolution of 2.7A. On the basis of the structure, and additional, biochemical studies, we provide possible reasons for the altered, properties of the mutant proteins, as well as highlight unique structural, features of the Rv1625c adenylyl cyclase.
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<StructureSection load='1yk9' size='340' side='right'caption='[[1yk9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YK9 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]] 2.7&#8491;</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=1yk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yk9 OCA], [https://pdbe.org/1yk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yk9 RCSB], [https://www.ebi.ac.uk/pdbsum/1yk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yk9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYA1_MYCTU CYA1_MYCTU]
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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/yk/1yk9_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=1yk9 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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The Rv1625c Class III adenylyl cyclase from Mycobacterium tuberculosis is a homodimeric enzyme with two catalytic centers at the dimer interface, and shows sequence similarity with the mammalian adenylyl and guanylyl cyclases. Mutation of the substrate-specifying residues in the catalytic domain of Rv1625c, either independently or together, to those present in guanylyl cyclases not only failed to confer guanylyl cyclase activity to the protein, but also severely abrogated the adenylyl cyclase activity of the enzyme. Biochemical analysis revealed alterations in the behavior of the mutants on ion-exchange chromatography, indicating differences in the surface-exposed charge upon mutation of substrate-specifying residues. The mutant proteins showed alterations in oligomeric status as compared to the wild-type enzyme, and differing abilities to heterodimerize with the wild-type protein. The crystal structure of a mutant has been solved to a resolution of 2.7A. On the basis of the structure, and additional biochemical studies, we provide possible reasons for the altered properties of the mutant proteins, as well as highlight unique structural features of the Rv1625c adenylyl cyclase.
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==About this Structure==
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A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis.,Ketkar AD, Shenoy AR, Ramagopal UA, Visweswariah SS, Suguna K J Mol Biol. 2006 Mar 3;356(4):904-16. Epub 2005 Dec 22. PMID:16403515<ref>PMID:16403515</ref>
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1YK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YK9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A structural basis for the role of nucleotide specifying residues in regulating the oligomerization of the Rv1625c adenylyl cyclase from M. tuberculosis., Ketkar AD, Shenoy AR, Ramagopal UA, Visweswariah SS, Suguna K, J Mol Biol. 2006 Mar 3;356(4):904-16. Epub 2005 Dec 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16403515 16403515]
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</div>
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[[Category: Adenylate cyclase]]
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<div class="pdbe-citations 1yk9" style="background-color:#fffaf0;"></div>
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Ketkar, A.D.]]
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[[Category: Ramagopal, U.A.]]
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[[Category: Shenoy, A.R.]]
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[[Category: Suguna, K.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: Visweswariah, S.S.]]
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[[Category: beta-alpha-beta sandwich]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:51:27 2007''
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==See Also==
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 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: Large Structures]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Ketkar AD]]
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[[Category: Ramagopal UA]]
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[[Category: Shenoy AR]]
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[[Category: Suguna K]]
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[[Category: Visweswariah SS]]

Current revision

Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c

PDB ID 1yk9

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