1luv

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(New page: 200px<br /> <applet load="1luv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1luv, resolution 1.85&Aring;" /> '''CATALYTIC AND STRUC...)
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[[Image:1luv.gif|left|200px]]<br />
 
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<applet load="1luv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1luv, resolution 1.85&Aring;" />
 
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'''CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS 30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE: INSERTION OF VAL CGAMMA INTO THE SUBSTRATE ACCESS CHANNEL'''<br />
 
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==Overview==
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==CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS 30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE: INSERTION OF VAL CGAMMA INTO THE SUBSTRATE ACCESS CHANNEL==
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Catalysis of the disproportionation of superoxide by human manganese, superoxide dismutase (MnSOD) is characterized by an initial burst of, catalysis followed by a much slower region that is zero order in, superoxide and due to a product inhibition by peroxide anion. We have, prepared site-specific mutants with replacements at His30, the side chain, of which lies along the substrate access channel and is about 5.8 A from, the metal. Using pulse radiolysis to generate superoxide, we have, determined that kcat/K(m) was decreased and product inhibition increased, for H30V MnSOD, both by 1-2 orders of magnitude, compared with wild type, H30N, and H30Q MnSOD. These effects are not attributed to the redox, potentials, which are similar for all of these variants. An investigation, of the crystal structure of H30V Mn(III)SOD compared with wild type, H30Q, and H30N Mn(III)SOD showed the positions of two gamma carbons of Val30 in, the active site; Cgamma1 overlaps Cgamma of His30 in wild type, and, Cgamma2 extends into the substrate access channel and occupies the, approximate position of a water molecule in the wild type. The data, suggest that Cgamma2 of the Val side chain has significantly interrupted, catalysis by this overlap into the access channel with possible overlap, with the substrate-product binding site. This is supported by comparison, of the crystal structure of H30V MnSOD with that of azide bound to, Mn(III)SOD from Thermus thermophilus and by visible absorption spectra, showing that azide binding to the metal in H30V Mn(III)SOD is abolished., Moreover, the presence of Val30 caused a 100-fold decrease in the rate, constant for dissociation of the product-inhibited complex compared with, wild type.
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<StructureSection load='1luv' size='340' side='right'caption='[[1luv]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1luv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LUV 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]] 1.85&#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=MN:MANGANESE+(II)+ION'>MN</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=1luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1luv OCA], [https://pdbe.org/1luv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1luv RCSB], [https://www.ebi.ac.uk/pdbsum/1luv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1luv ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/SODM_HUMAN SODM_HUMAN] Genetic variation in SOD2 is associated with susceptibility to microvascular complications of diabetes type 6 (MVCD6) [MIM:[https://omim.org/entry/612634 612634]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
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== Function ==
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[https://www.uniprot.org/uniprot/SODM_HUMAN SODM_HUMAN] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:10334867</ref>
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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/lu/1luv_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=1luv 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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1LUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN 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=1LUV OCA].
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel., Hearn AS, Stroupe ME, Cabelli DE, Ramilo CA, Luba JP, Tainer JA, Nick HS, Silverman DN, Biochemistry. 2003 Mar 18;42(10):2781-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12627943 12627943]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Superoxide dismutase]]
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[[Category: Cabelli DE]]
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[[Category: Cabelli, D.E.]]
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[[Category: Hearn AS]]
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[[Category: Hearn, A.S.]]
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[[Category: Luba JP]]
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[[Category: Luba, J.P.]]
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[[Category: Ramilo CA]]
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[[Category: Ramilo, C.A.]]
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[[Category: Silverman DN]]
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[[Category: Silverman, D.N.]]
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[[Category: Stroupe ME]]
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[[Category: Stroupe, M.E.]]
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[[Category: Tainer JA]]
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[[Category: Tainer, J.A.]]
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[[Category: MN]]
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[[Category: high resolution]]
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[[Category: human manganese superoxide dismutase]]
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[[Category: mn]]
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[[Category: mnsod]]
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[[Category: wild type]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:04:19 2007''
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Current revision

CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS 30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE: INSERTION OF VAL CGAMMA INTO THE SUBSTRATE ACCESS CHANNEL

PDB ID 1luv

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