1snm

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(New page: 200px<br /><applet load="1snm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1snm, resolution 1.74&Aring;" /> '''ACTIVE SITE MUTANT G...)
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[[Image:1snm.gif|left|200px]]<br /><applet load="1snm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1snm, resolution 1.74&Aring;" />
 
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'''ACTIVE SITE MUTANT GLU-43 (RIGHT ARROW) ASP IN STAPHYLOCOCCAL NUCLEASE DISPLAYS NONLOCAL STRUCTURAL CHANGES'''<br />
 
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==Overview==
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==ACTIVE SITE MUTANT GLU-43 (RIGHT ARROW) ASP IN STAPHYLOCOCCAL NUCLEASE DISPLAYS NONLOCAL STRUCTURAL CHANGES==
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The crystal structure of the Glu-43----Asp mutant of staphylococcal, nuclease complexed with Ca2+ and the inhibitor thymidine, 3',5'-bisphosphate (pdTp) has been determined and refined by restrained, least-squares methods to a conventional crystallographic R value of 0.174, at a resolution of 1.74 A. Throughout most of the structure, the, conformation of the backbone atoms of the mutant is similar to that of the, wild-type protein; however, the seemingly conservative mutation Glu----Asp, has significantly perturbed the structure of a loop adjacent to the active, site, as well as giving rise to looser binding of the essential calcium, ion and to a less extensive network of bound water molecules in the active, site. Crystal contacts that extend into the active site have also been, altered by this amino acid substitution. The changes caused by this, mutation are considerably more drastic than would have been predicted and, should serve as caveats to those who would draw conclusions about, structure-function relationships on the basis of site-directed mutagenesis, experiments in the absence of structural data.
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<StructureSection load='1snm' size='340' side='right'caption='[[1snm]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1snm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SNM 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]] 1.74&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</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=1snm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1snm OCA], [https://pdbe.org/1snm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1snm RCSB], [https://www.ebi.ac.uk/pdbsum/1snm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1snm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NUC_STAAU NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
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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/sn/1snm_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=1snm 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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1SNM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CA and THP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SNM OCA].
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*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Active site mutant Glu-43----Asp in staphylococcal nuclease displays nonlocal structural changes., Loll PJ, Lattman EE, Biochemistry. 1990 Jul 24;29(29):6866-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2397218 2397218]
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[[Category: Large Structures]]
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[[Category: Micrococcal nuclease]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Lattman, E.E.]]
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[[Category: Lattman EE]]
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[[Category: Loll, P.J.]]
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[[Category: Loll PJ]]
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[[Category: CA]]
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[[Category: THP]]
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[[Category: hydrolase (phosphoric diester)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:30:46 2007''
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ACTIVE SITE MUTANT GLU-43 (RIGHT ARROW) ASP IN STAPHYLOCOCCAL NUCLEASE DISPLAYS NONLOCAL STRUCTURAL CHANGES

PDB ID 1snm

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