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1x9i

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[[Image:1x9i.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate==
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|PDB= 1x9i |SIZE=350|CAPTION= <scene name='initialview01'>1x9i</scene>, resolution 1.16&Aring;
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<StructureSection load='1x9i' size='340' side='right'caption='[[1x9i]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1x9i]] 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=1X9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X9I FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.16&#8491;</td></tr>
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|GENE= PAE1610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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}}
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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=1x9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9i OCA], [https://pdbe.org/1x9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x9i RCSB], [https://www.ebi.ac.uk/pdbsum/1x9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9i 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/x9/1x9i_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=1x9i 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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'''Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1x9i" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1X9I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9I OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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://www.ncbi.nlm.nih.gov/pubmed/15518558 15518558]
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[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]
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[[Category: Single protein]]
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[[Category: Davies C]]
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[[Category: Davies, C.]]
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[[Category: Hansen T]]
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[[Category: Hansen, T]]
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[[Category: Schoenheit P]]
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[[Category: Schoenheit, P.]]
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[[Category: Swan MK]]
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[[Category: Swan, M K.]]
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[[Category: G6Q]]
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[[Category: GOL]]
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[[Category: crenarchaeon]]
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[[Category: enzyme]]
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[[Category: glucose 6-phosphate]]
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[[Category: hyperthermophile]]
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[[Category: pgi superfamily]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:06:49 2008''
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Current revision

Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate

PDB ID 1x9i

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