This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3bjz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:44, 12 January 2022) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3bjz.jpg|left|200px]]<br /><applet load="3bjz" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="3bjz, resolution 2.40&Aring;" />
 
-
'''Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase'''<br />
 
-
==Overview==
+
==Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase==
-
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.
+
<StructureSection load='3bjz' size='340' side='right'caption='[[3bjz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3bjz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BJZ FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x92|1x92]], [[2i22|2i22]], [[2i2w|2i2w]]</div></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gmhA, PA4425 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=3bjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bjz OCA], [https://pdbe.org/3bjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bjz RCSB], [https://www.ebi.ac.uk/pdbsum/3bjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bjz ProSAT], [https://www.topsan.org/Proteins/MCSG/3bjz TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/3bjz_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</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/main_output.php?pdb_ID=3bjz ConSurf].
 +
<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.
-
==About this Structure==
+
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>
-
3BJZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4 Binding Site For Residue A 198'>AC1</scene>, <scene name='pdbsite=AC2:So4 Binding Site For Residue B 198'>AC2</scene>, <scene name='pdbsite=AC3:So4 Binding Site For Residue C 198'>AC3</scene> and <scene name='pdbsite=AC4:So4 Binding Site For Residue D 198'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BJZ OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18056714 18056714]
+
</div>
-
[[Category: Pseudomonas aeruginosa pao1]]
+
<div class="pdbe-citations 3bjz" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Evdokimova, E.]]
+
<references/>
-
[[Category: Joachimiak, A.]]
+
__TOC__
-
[[Category: Kudritska, M.]]
+
</StructureSection>
-
[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
+
[[Category: Large Structures]]
-
[[Category: Osipiuk, J.]]
+
[[Category: Pseae]]
-
[[Category: Savchenko, A.]]
+
[[Category: Evdokimova, E]]
-
[[Category: Walker, J.R.]]
+
[[Category: Joachimiak, A]]
-
[[Category: CL]]
+
[[Category: Kudritska, M]]
-
[[Category: SO4]]
+
[[Category: Structural genomic]]
-
[[Category: alpha/beta protein]]
+
[[Category: Osipiuk, J]]
-
[[Category: carbohydrate metabolism]]
+
[[Category: Savchenko, A]]
-
[[Category: cytoplasm]]
+
[[Category: Walker, J R]]
-
[[Category: isomerase]]
+
[[Category: Alpha/beta protein]]
-
[[Category: lipopolysaccharide biosynthesis]]
+
[[Category: Carbohydrate metabolism]]
-
[[Category: mcsg]]
+
[[Category: Cytoplasm]]
-
[[Category: midwest center for structural genomics]]
+
[[Category: Isomerase]]
-
[[Category: protein structure initiative]]
+
[[Category: Lipopolysaccharide biosynthesis]]
-
[[Category: psi]]
+
[[Category: Mcsg]]
-
[[Category: sis domain]]
+
[[Category: PSI, Protein structure initiative]]
-
 
+
[[Category: Sis domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:02:38 2008''
+

Current revision

Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase

PDB ID 3bjz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bjz"
Personal tools