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1ids

From Proteopedia

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(New page: 200px<br /><applet load="1ids" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ids, resolution 2.0&Aring;" /> '''X-RAY STRUCTURE ANALY...)
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[[Image:1ids.jpg|left|200px]]<br /><applet load="1ids" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ids, resolution 2.0&Aring;" />
 
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'''X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS'''<br />
 
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==Overview==
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==X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS==
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The X-ray structure of the tetrameric iron-dependent superoxide dismutase, from Mycobacterium tuberculosis has been refined to an R-factor of 0.167, and a correlation coefficient of 0.954 at 2.0 A resolution. The crystals, are monoclinic P2(1) and have four subunits related by strong, non-crystallographic 222 (or D2) symmetry in the asymmetric unit. 198 of, the 207 amino acids of each subunit are defined by the electron density, which shows that they adopt the conserved fold of other iron- or, manganese-dependent SODs. The structure can be divided into two domains, the N-terminal domain involving an extended region followed by two, projecting antiparallel alpha-helices, and the C-terminal domain, containing four more helical segments with a three-stranded antiparallel, beta-sheet inserted sequentially between the fourth and fifth helices. The, catalytic iron is co-ordinated by five ligands: three histidines (residues, 28, 76 and 164), one aspartate (160) and a solvent molecule. The inferred, positions of protons at the active site are consistent with the solvent, ligand being a hydroxide ion. This ligand interacts with His145 in the, Mycobacterium tuberculosis SOD. In the highly homologous Mycobacterium, leprae Mn-SOD, the histidine is replaced by glutamine, this being the only, significant residue difference within 10 A of the Fe3+. The nature of the, amino acid at this position may influence the metal ion specificity of, these enzymes. The subunits of the Mycobacterium tuberculosis SOD, associate by polar contacts to form dimers, which closely resemble those, of other dimeric or tetrameric Fe- or Mn-SODs. However, the dimer-dimer, interactions within the tetramer are novel, being dominated by, dimerisation of the 144 to 152 loop regions which connect the outer two, beta-strands of the three-membered beta-sheet. This contrasts strongly, with the other tetrameric Fe- or Mn-SODs where the dimer-dimer association, is dominated by the projecting alpha alpha-turn in the N-terminal domain.
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<StructureSection load='1ids' size='340' side='right'caption='[[1ids]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ids]] is a 4 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=1IDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDS 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&#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=FE:FE+(III)+ION'>FE</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=1ids FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ids OCA], [https://pdbe.org/1ids PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ids RCSB], [https://www.ebi.ac.uk/pdbsum/1ids PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ids ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SODF_MYCTU SODF_MYCTU] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
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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/id/1ids_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=1ids 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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1IDS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDS OCA].
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions., Cooper JB, McIntyre K, Badasso MO, Wood SP, Zhang Y, Garbe TR, Young D, J Mol Biol. 1995 Mar 3;246(4):531-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7877174 7877174]
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[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Cooper JB]]
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[[Category: Superoxide dismutase]]
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[[Category: Mcintyre K]]
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[[Category: Cooper, J.B.]]
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[[Category: Wood SP]]
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[[Category: Mcintyre, K.]]
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[[Category: Young D]]
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[[Category: Wood, S.P.]]
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[[Category: Zhang Y]]
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[[Category: Young, D.]]
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[[Category: Zhang, Y.]]
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[[Category: FE]]
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[[Category: superoxide dismutase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:19:21 2007''
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Current revision

X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS

PDB ID 1ids

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