1gpw
From Proteopedia
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|PDB= 1gpw |SIZE=350|CAPTION= <scene name='initialview01'>1gpw</scene>, resolution 2.40Å | |PDB= 1gpw |SIZE=350|CAPTION= <scene name='initialview01'>1gpw</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=PO1:Binding+Site+For+Po4+P6'>PO1</scene> | |SITE= <scene name='pdbsite=PO1:Binding+Site+For+Po4+P6'>PO1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpw OCA], [http://www.ebi.ac.uk/pdbsum/1gpw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpw RCSB]</span> | ||
}} | }} | ||
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[[Category: Walker, M.]] | [[Category: Walker, M.]] | ||
[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
| - | [[Category: PO4]] | ||
[[Category: ammonia channel]] | [[Category: ammonia channel]] | ||
[[Category: cyclase]] | [[Category: cyclase]] | ||
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[[Category: histidine biosynthesis]] | [[Category: histidine biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:59 2008'' |
Revision as of 17:49, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL EVIDENCE FOR AMMONIA TUNNELING ACROSS THE (BETA/ALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE BIENZYME COMPLEX.
Overview
Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold.
About this Structure
1GPW is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex., Douangamath A, Walker M, Beismann-Driemeyer S, Vega-Fernandez MC, Sterner R, Wilmanns M, Structure. 2002 Feb;10(2):185-93. PMID:11839304
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