1lu4

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(New page: 200px<br /><applet load="1lu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lu4, resolution 1.12&Aring;" /> '''1.1 ANGSTROM RESOLUT...)
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[[Image:1lu4.gif|left|200px]]<br /><applet load="1lu4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lu4, resolution 1.12&Aring;" />
 
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'''1.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED MYCOBACTERIUM TUBERCULOSIS DISULFIDE OXIDOREDUCTASE HOMOLOGOUS TO E. COLI DSBE: IMPLICATIONS FOR FUNCTIONS'''<br />
 
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==Overview==
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==1.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED MYCOBACTERIUM TUBERCULOSIS DISULFIDE OXIDOREDUCTASE HOMOLOGOUS TO E. COLI DSBE: IMPLICATIONS FOR FUNCTIONS==
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Mycobacterium tuberculosis, a Gram-positive bacterium, encodes a secreted, Dsb-like protein annotated as Mtb DsbE (Rv2878c, also known as MPT53)., Because Dsb proteins in Escherichia coli and other bacteria seem to, catalyze proper folding during protein secretion and because folding of, secreted proteins is thought to be coupled to disulfide oxidoreduction, the function of Mtb DsbE may be to ensure that secreted proteins are in, their correctly folded states. We have determined the crystal structure of, Mtb DsbE to 1.1 A resolution, which reveals a thioredoxin-like domain with, a typical CXXC active site. These cysteines are in their reduced state., Biochemical characterization of Mtb DsbE reveals that this disulfide, oxidoreductase is an oxidant, unlike Gram-negative bacteria DsbE proteins, which have been shown to be weak reductants. In addition, the pK(a) value, of the active site, solvent-exposed cysteine is approximately 2 pH units, lower than that of Gram-negative DsbE homologs. Finally, the reduced form, of Mtb DsbE is more stable than the oxidized form, and Mtb DsbE is able to, oxidatively fold hirudin. Structural and biochemical analysis implies that, Mtb DsbE functions differently from Gram-negative DsbE homologs, and we, discuss its possible functional role in the bacterium.
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<StructureSection load='1lu4' size='340' side='right'caption='[[1lu4]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lu4]] 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=1LU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LU4 FirstGlance]. <br>
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1LU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LU4 OCA].
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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]] 1.12&#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=1lu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu4 OCA], [https://pdbe.org/1lu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lu4 RCSB], [https://www.ebi.ac.uk/pdbsum/1lu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lu4 ProSAT], [https://www.topsan.org/Proteins/TBSGC/1lu4 TOPSAN]</span></td></tr>
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==Reference==
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</table>
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Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis., Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D, J Biol Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14597624 14597624]
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== Function ==
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[https://www.uniprot.org/uniprot/MPT53_MYCTU MPT53_MYCTU] Disulfide oxidoreductase that catalyzes the oxidation of reduced, unfolded secreted proteins to form disulfide bonds. Despite a weak homology to thioredoxin this cannot serve as a substrate for thioredoxin reductase.<ref>PMID:14597624</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/1lu4_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=1lu4 ConSurf].
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<div style="clear:both"></div>
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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]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Apostol MI]]
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[[Category: Apostol, M.I.]]
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[[Category: Bardwell J]]
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[[Category: Bardwell, J.]]
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[[Category: Eisenberg D]]
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[[Category: Eisenberg, D.]]
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[[Category: Gennaro M]]
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[[Category: Gennaro, M.]]
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[[Category: Gleiter S]]
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[[Category: Gleiter, S.]]
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[[Category: Goulding CW]]
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[[Category: Goulding, C.W.]]
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[[Category: Parseghian A]]
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[[Category: Parseghian, A.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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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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[[Category: thioredoxin-like fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:53:18 2007''
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Current revision

1.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED MYCOBACTERIUM TUBERCULOSIS DISULFIDE OXIDOREDUCTASE HOMOLOGOUS TO E. COLI DSBE: IMPLICATIONS FOR FUNCTIONS

PDB ID 1lu4

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