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1x9h

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(New page: 200px<br /><applet load="1x9h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9h, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:1x9h.jpg|left|200px]]<br /><applet load="1x9h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1x9h, resolution 1.50&Aring;" />
 
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'''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate'''<br />
 
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==Overview==
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==Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate==
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The crystal structure of a dual-specificity phosphoglucose/phosphomannose, isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has, been determined in complex with glucose 6-phosphate at 1.16 A resolution, and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of, mannose 6-phosphate (M6P) into the active site of the enzyme shows that, the PMI activity of this enzyme may be due to the additional space, imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a, glutamine. The increased space may permit rotation of the C2-C3 bond in, M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a, further C2-C3 rotation of the resulting cis-enediolate, re-donation of a, proton to C1 by the same residue. A proline residue (in place of a glycine, in PGI) may also promote PMI activity by positioning the C1-O1 region of, M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol, mechanism of catalysis, and this activity appears to arise from a subtle, difference in the architecture of the enzyme, compared to bacterial and, eukaryotic PGIs.
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<StructureSection load='1x9h' size='340' side='right'caption='[[1x9h]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1x9h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X9H 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]] 1.5&#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=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1x9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9h OCA], [https://pdbe.org/1x9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x9h RCSB], [https://www.ebi.ac.uk/pdbsum/1x9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PGMI_PYRAE PGMI_PYRAE] Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
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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/x9/1x9h_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=1x9h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a glutamine. The increased space may permit rotation of the C2-C3 bond in M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a further C2-C3 rotation of the resulting cis-enediolate, re-donation of a proton to C1 by the same residue. A proline residue (in place of a glycine in PGI) may also promote PMI activity by positioning the C1-O1 region of M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol mechanism of catalysis, and this activity appears to arise from a subtle difference in the architecture of the enzyme, compared to bacterial and eukaryotic PGIs.
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==About this Structure==
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Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes.,Swan MK, Hansen T, Schonheit P, Davies C Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:15518558<ref>PMID:15518558</ref>
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1X9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with SO4, F6R and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X9H OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15518558 15518558]
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</div>
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[[Category: Pyrobaculum aerophilum]]
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<div class="pdbe-citations 1x9h" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Davies, C.]]
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[[Category: Hansen, T]]
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[[Category: Schoenheit, P.]]
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[[Category: Swan, M.K.]]
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[[Category: F6R]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: crenarchaeon]]
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[[Category: enzyme]]
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[[Category: fructose 6-phosphate]]
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[[Category: hyperthermophile]]
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[[Category: pgi superfamily]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:54:56 2007''
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==See Also==
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*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
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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]]
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[[Category: Pyrobaculum aerophilum]]
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[[Category: Davies C]]
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[[Category: Hansen T]]
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[[Category: Schoenheit P]]
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[[Category: Swan MK]]

Current revision

Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate

PDB ID 1x9h

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