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5lu6

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Heptose isomerase mutant - H64Q

Structural highlights

5lu6 is a 4 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.67Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GMHA_BURPS Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.^[1]

Publication Abstract from PubMed

Cooperativity is a feature many multimeric proteins use to control activity. Here we show that the bacterial heptose isomerase GmhA displays homotropic positive and negative cooperativity among its four protomers. Most similar proteins achieve this through conformational changes: GmhA instead employs a delicate network of hydrogen bonds, and couples pairs of active sites controlled by a unique water channel. This network apparently raises the Lewis acidity of the catalytic zinc, thus increasing the activity at one active site at the cost of preventing substrate from adopting a reactive conformation at the paired negatively cooperative site - a "half-site" behavior. Our study establishes the principle that multimeric enzymes can exploit this cooperativity without conformational changes to maximize their catalytic power and control. More broadly, this subtlety by which enzymes regulate functions could be used to explore new inhibitor design strategies.

A half-site multimeric enzyme achieves its cooperativity without conformational changes.,Vivoli M, Pang J, Harmer NJ Sci Rep. 2017 Nov 28;7(1):16529. doi: 10.1038/s41598-017-16421-2. PMID:29184087^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Harmer NJ. The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site. J Mol Biol. 2010 Jul 16;400(3):379-92. Epub 2010 May 4. PMID:20447408 doi:10.1016/j.jmb.2010.04.058
↑ Vivoli M, Pang J, Harmer NJ. A half-site multimeric enzyme achieves its cooperativity without conformational changes. Sci Rep. 2017 Nov 28;7(1):16529. doi: 10.1038/s41598-017-16421-2. PMID:29184087 doi:http://dx.doi.org/10.1038/s41598-017-16421-2

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lu6"

Categories: Burkholderia pseudomallei | Large Structures | Harmer NJ | Pang J | Vivoli M

@@ Line 3: / Line 3: @@
 <StructureSection load='5lu6' size='340' side='right'caption='[[5lu6]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lu6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LU6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lu6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LU6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.67&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gmhA, DP49_467 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=I22:D-ALTRO-HEPT-2-ULOSE+7-PHOSPHATE'>I22</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-sedoheptulose_7-phosphate_isomerase D-sedoheptulose 7-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.28 5.3.1.28] </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=5lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lu6 OCA], [https://pdbe.org/5lu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lu6 RCSB], [https://www.ebi.ac.uk/pdbsum/5lu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lu6 ProSAT]</span></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=5lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lu6 OCA], [http://pdbe.org/5lu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lu6 RCSB], [http://www.ebi.ac.uk/pdbsum/5lu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lu6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A095TT41_BURPE A0A095TT41_BURPE]] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.[HAMAP-Rule:MF_00067][SAAS:SAAS00846114]
+[https://www.uniprot.org/uniprot/GMHA_BURPS GMHA_BURPS] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.<ref>PMID:20447408</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus pseudomallei whitmore 1913]]
+[[Category: Burkholderia pseudomallei]]
-[[Category: D-sedoheptulose 7-phosphate isomerase]]
 [[Category: Large Structures]]
-[[Category: Harmer, N J]]
+[[Category: Harmer NJ]]
-[[Category: Pang, J]]
+[[Category: Pang J]]
-[[Category: Vivoli, M]]
+[[Category: Vivoli M]]
-[[Category: Cooperativity]]
-[[Category: Enzyme kinetic]]
-[[Category: Hydrogen bond]]
-[[Category: Isomerase]]
-[[Category: Molecular modelling]]
-[[Category: Quantum mechanic]]

5lu6

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Current revision

Heptose isomerase mutant - H64Q

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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