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==CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA PHOSPHOHEPTOSE ISOMERASE IN COMPLEX WITH REACTION PRODUCT D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE==
==CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA PHOSPHOHEPTOSE ISOMERASE IN COMPLEX WITH REACTION PRODUCT D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE==
<StructureSection load='1x92' size='340' side='right' caption='[[1x92]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1x92' size='340' side='right'caption='[[1x92]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1x92]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X92 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1x92]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X92 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M7P:D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE'>M7P</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpcA, gmhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M7P:D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE'>M7P</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x92 OCA], [http://pdbe.org/1x92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x92 RCSB], [http://www.ebi.ac.uk/pdbsum/1x92 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x92 OCA], [https://pdbe.org/1x92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x92 RCSB], [https://www.ebi.ac.uk/pdbsum/1x92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x92 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GMHA_PSEAE GMHA_PSEAE]] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate (By similarity).  
[https://www.uniprot.org/uniprot/GMHA_PSEAE GMHA_PSEAE] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x9/1x92_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x9/1x92_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1x92 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The barrier imposed by lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria presents a significant challenge in treatment of these organisms with otherwise effective hydrophobic antibiotics. The absence of L-glycero-D-manno-heptose in the LPS molecule is associated with a dramatically increased bacterial susceptibility to hydrophobic antibiotics and thus enzymes in the ADP-heptose biosynthesis pathway are of significant interest. GmhA catalyzes the isomerization of D-sedoheptulose 7-phosphate into D-glycero-D-manno-heptose 7-phosphate, the first committed step in the formation of ADP-heptose. Here we report structures of GmhA from Escherichia coli and Pseudomonas aeruginosa in apo, substrate, and product-bound forms, which together suggest that GmhA adopts two distinct conformations during isomerization through reorganization of quaternary structure. Biochemical characterization of GmhA mutants, combined with in vivo analysis of LPS biosynthesis and novobiocin susceptibility, identifies key catalytic residues. We postulate GmhA acts through an enediol-intermediate isomerase mechanism.
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants.,Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS J Biol Chem. 2008 Feb 1;283(5):2835-45. Epub 2007 Dec 3. PMID:18056714<ref>PMID:18056714</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1x92" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Edwards, A]]
[[Category: Large Structures]]
[[Category: Evdokimova, E]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Joachimiak, A]]
[[Category: Edwards A]]
[[Category: Kudritska, M]]
[[Category: Evdokimova E]]
[[Category: Structural genomic]]
[[Category: Joachimiak A]]
[[Category: Savchenko, A]]
[[Category: Kudritska M]]
[[Category: Walker, J R]]
[[Category: Savchenko A]]
[[Category: A/b protein]]
[[Category: Walker JR]]
[[Category: Isomerase]]
[[Category: Lipopolysaccharide biosynthesis]]
[[Category: Mcsg]]
[[Category: PSI, Protein structure initiative]]
[[Category: Sis domain]]

Latest revision as of 11:48, 14 February 2024

CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA PHOSPHOHEPTOSE ISOMERASE IN COMPLEX WITH REACTION PRODUCT D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATECRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA PHOSPHOHEPTOSE ISOMERASE IN COMPLEX WITH REACTION PRODUCT D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE

Structural highlights

1x92 is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GMHA_PSEAE Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1x92, resolution 2.30Å

Drag the structure with the mouse to rotate

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