1em1

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[[Image:1em1.jpg|left|200px]]<br /><applet load="1em1" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1em1, resolution 2.13&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE, Q143A'''<br />
 
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==Overview==
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==X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE, Q143A==
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Glutamine 143 in human manganese superoxide dismutase (MnSOD) forms a, hydrogen bond with the manganese-bound solvent molecule and is, investigated by replacement using site-specific mutagenesis. Crystal, structures showed that the replacement of Gln 143 with Ala made no, significant change in the overall structure of the mutant enzyme. Two new, water molecules in Q143A MnSOD were situated in positions nearly identical, with the Oepsilon1 and Nepsilon2 of the replaced Gln 143 side chain and, maintained a hydrogen-bonded network connecting the manganese-bound, solvent molecule to other residues in the active site. However, their, presence could not sustain the stability and activity of the enzyme; the, main unfolding transition of Q143A was decreased 16 degrees C and its, catalysis decreased 250-fold to k(cat)/K(m) = 3 x 10(6) M(-)(1) s(-)(1), as determined by stopped-flow spectrophotometry and pulse radiolysis. The, mutant Q143A MnSOD and other mutants at position 143 showed very low, levels of product inhibition and favored Mn(II)SOD in the resting state, whereas the wild type showed strong product inhibition and favored, Mn(III)SOD. However, these differences did not affect the rate constant, for dissociation of the product-inhibited complex in Q143A MnSOD which was, determined from a characteristic absorbance at 420 nm and was comparable, in magnitude ( approximately 100 s(-)(1)) to that of the wild-type enzyme., Hence, Gln 143, which is necessary for maximal activity in superoxide, dismutation, appears to have no role in stabilization and dissociation of, the product-inhibited complex.
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<StructureSection load='1em1' size='340' side='right'caption='[[1em1]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1em1]] 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=1EM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EM1 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]] 2.13&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1em1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1em1 OCA], [https://pdbe.org/1em1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1em1 RCSB], [https://www.ebi.ac.uk/pdbsum/1em1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1em1 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/em/1em1_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=1em1 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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1EM1 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EM1 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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Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis., Leveque VJ, Stroupe ME, Lepock JR, Cabelli DE, Tainer JA, Nick HS, Silverman DN, Biochemistry. 2000 Jun 20;39(24):7131-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10852710 10852710]
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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: Lepock JR]]
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[[Category: Lepock, J.R.]]
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[[Category: Leveque V]]
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[[Category: Leveque, V.]]
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[[Category: Nick HS]]
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[[Category: Nick, H.S.]]
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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: SO4]]
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[[Category: alpha-beta protein]]
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[[Category: metalloenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:44:05 2008''
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Current revision

X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE, Q143A

PDB ID 1em1

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