1ecj
From Proteopedia
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| - | [[Image:1ecj.jpg|left|200px]] | + | [[Image:1ecj.jpg|left|200px]] |
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| - | '''ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 AMP PER TETRAMER''' | + | {{Structure |
| + | |PDB= 1ecj |SIZE=350|CAPTION= <scene name='initialview01'>1ecj</scene>, resolution 2.5Å | ||
| + | |SITE= <scene name='pdbsite=NTA:Ntn+Amidotransferase+Active+Site'>NTA</scene>, <scene name='pdbsite=NTB:Ntn+Amidotransferase+Active+Site'>NTB</scene>, <scene name='pdbsite=NTC:Ntn+Amidotransferase+Active+Site'>NTC</scene>, <scene name='pdbsite=NTD:Ntn+Amidotransferase+Active+Site'>NTD</scene>, <scene name='pdbsite=PRA:Phosphoribosyl+transf.+Active+Site.+The+Active+Site+In+T+...'>PRA</scene>, <scene name='pdbsite=PRB:Phosphoribosyl+transf.+Active+Site.+The+Active+Site+In+T+...'>PRB</scene>, <scene name='pdbsite=PRC:Phosphoribosyl+transf.+Active+Site.+The+Active+Site+In+T+...'>PRC</scene> and <scene name='pdbsite=PRT:Phosphoribosyl+transf.+Active+Site.+The+Active+Site+In+T+...'>PRT</scene> | ||
| + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Amidophosphoribosyltransferase Amidophosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.14 2.4.2.14] | ||
| + | |GENE= PURF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 AMP PER TETRAMER''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ECJ is a [ | + | 1ECJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECJ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli., Muchmore CR, Krahn JM, Kim JH, Zalkin H, Smith JL, Protein Sci. 1998 Jan;7(1):39-51. PMID:[http:// | + | Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli., Muchmore CR, Krahn JM, Kim JH, Zalkin H, Smith JL, Protein Sci. 1998 Jan;7(1):39-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9514258 9514258] |
[[Category: Amidophosphoribosyltransferase]] | [[Category: Amidophosphoribosyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:39 2008'' |
Revision as of 08:53, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | PURF (Escherichia coli) | ||||||
| Activity: | Amidophosphoribosyltransferase, with EC number 2.4.2.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 AMP PER TETRAMER
Overview
Crystal structures of glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase from Escherichia coli have been determined to 2.0-A resolution in the absence of ligands, and to 2.5-A resolution with the feedback inhibitor AMP bound to the PRPP catalytic site. Glutamine PRPP amidotransferase (GPATase) employs separate catalytic domains to abstract nitrogen from the amide of glutamine and to transfer nitrogen to the acceptor substrate PRPP. The unliganded and AMP-bound structures, which are essentially identical, are interpreted as the inhibited form of the enzyme because the two active sites are disconnected and the PRPP active site is solvent exposed. The structures were compared with a previously reported 3.0-A structure of the homologous Bacillus subtilis enzyme (Smith JL et al., 1994, Science 264:1427-1433). The comparison indicates a pattern of conservation of peptide structures involved with catalysis and variability in enzyme regulatory functions. Control of glutaminase activity, communication between the active sites, and regulation by feedback inhibitors are addressed differently by E. coli and B. subtilis GPATases. The E. coli enzyme is a prototype for the metal-free GPATases, whereas the B. subtilis enzyme represents the metal-containing enzymes. The structure of the E. coli enzyme suggests that a common ancestor of the two enzyme subfamilies may have included an Fe-S cluster.
About this Structure
1ECJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli., Muchmore CR, Krahn JM, Kim JH, Zalkin H, Smith JL, Protein Sci. 1998 Jan;7(1):39-51. PMID:9514258
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