1ecf
From Proteopedia
(New page: 200px<br /><applet load="1ecf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ecf, resolution 2.0Å" /> '''ESCHERICHIA COLI GLUT...) |
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| - | [[Image:1ecf.jpg|left|200px]]<br /><applet load="1ecf" size=" | + | [[Image:1ecf.jpg|left|200px]]<br /><applet load="1ecf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ecf, resolution 2.0Å" /> | caption="1ecf, resolution 2.0Å" /> | ||
'''ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE'''<br /> | '''ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of glutamine phosphoribosylpyrophosphate (PRPP) | + | 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== | ==About this Structure== | ||
| - | 1ECF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PIN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1ECF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PIN:'>PIN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Krahn, J | + | [[Category: Krahn, J M.]] |
[[Category: PIN]] | [[Category: PIN]] | ||
[[Category: glutamine amidotransferase]] | [[Category: glutamine amidotransferase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:17 2008'' |
Revision as of 10:26, 21 February 2008
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ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE
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
1ECF is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Amidophosphoribosyltransferase, with EC number 2.4.2.14 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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