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1hox

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Revision as of 06:48, 5 April 2017

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE

Structural highlights

1hox is a 2 chain structure with sequence from Oryctolagus cuniculus. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2pgi, 1pgi, 1boz, 1dqr, 1g98, 1hm5
Activity:	Glucose-6-phosphate isomerase, with EC number 5.3.1.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[G6PI_RABIT] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons (By similarity).

Evolutionary Conservation

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

Publication Abstract from PubMed

Phosphoglucose isomerase (PGI, EC 5.3.1.9) catalyzes the interconversion of D-glucose 6-phosphate (G6P) and D-fructose 6-phosphate (F6P) and plays important roles in glycolysis and gluconeogenesis. Biochemical characterization of the enzyme has led to a proposed multistep catalytic mechanism. First, the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. Catalysis proceeds in both the G6P to F6P and F6P to G6P directions, so both G6P and F6P are substrates. X-ray crystal structure analysis of rabbit and bacterial PGI has previously identified the location of the enzyme active site, and a recent crystal structure of rabbit PGI identified Glu357 as a candidate functional group for transferring the proton. However, it was not clear which active site amino acid residues catalyze the ring opening step. In this paper, we report the X-ray crystal structure of rabbit PGI complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution. The location of the substrate relative to the side chains of His388 suggest that His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2. Comparison to a structure of rabbit PGI with 5PAA bound indicates that ring opening is followed by loss of the protonated water molecule and conformational changes in the substrate and the protein so that a helix containing amino acids 513-520 moves in toward the substrate to form additional hydrogen bonds with the substrate.

Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate.,Lee JH, Chang KZ, Patel V, Jeffery CJ Biochemistry. 2001 Jul 3;40(26):7799-805. PMID:11425306^[1]

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

References

↑ Lee JH, Chang KZ, Patel V, Jeffery CJ. Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate. Biochemistry. 2001 Jul 3;40(26):7799-805. PMID:11425306

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hox"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE==
 <StructureSection load='1hox' size='340' side='right' caption='[[1hox]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pgi|2pgi]], [[1pgi|1pgi]], [[1boz|1boz]], [[1dqr|1dqr]], [[1g98|1g98]], [[1hm5|1hm5]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </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=1hox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hox OCA], [http://pdbe.org/1hox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hox RCSB], [http://www.ebi.ac.uk/pdbsum/1hox PDBsum]</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=1hox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hox OCA], [http://pdbe.org/1hox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hox RCSB], [http://www.ebi.ac.uk/pdbsum/1hox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hox ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/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=1hox ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1hox

From Proteopedia

Revision as of 06:48, 5 April 2017

CRYSTAL STRUCTURE OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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