1ecc
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1ECC 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 MN, ONL and PCP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1ECC 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 MN, ONL and PCP as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Sites: NTA, NTB, PRB and PRT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ECC OCA]]. |
==Reference== | ==Reference== | ||
Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site., Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL, Biochemistry. 1997 Sep 16;36(37):11061-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9333323 9333323] | Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site., Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL, Biochemistry. 1997 Sep 16;36(37):11061-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9333323 9333323] | ||
| + | [[Category: Amidophosphoribosyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:39:09 2007'' |
Revision as of 08:34, 30 October 2007
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ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH MN-CPRPP AND 5-OXO-NORLEUCINE
Overview
Activation of gluatmine phosphoribosylpyrophosphate (RPPP), amidotransferase (GPATase) by binding of a PRPP substrate analog results, in the formation of a 20 A channel connecting the active site for, glutamine hydrolysis in one domain with the PRPP site in a second domain., This solvent-inaccessible channel permits transfer of the NH3 intermediate, between the two active sites. Tunneling of NH3 may be a common mechanism, for glutamine amidotransferase-catalyzed nitrogen transfer and for, coordination of catalysis at two distinct active sites in complex enzymes., The 2.4 A crystal structure of the active conformer of GPATase also, provides the first description of an intact active site for the, phosphoribosyltransferase (PRTase) family of nucleotide synthesis and, salvage enzymes. ... [(full description)]
About this Structure
1ECC is a [Single protein] structure of sequence from [Escherichia coli] with MN, ONL and PCP as [ligands]. Active as [Amidophosphoribosyltransferase], with EC number [2.4.2.14]. Structure known Active Sites: NTA, NTB, PRB and PRT. Full crystallographic information is available from [OCA].
Reference
Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site., Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL, Biochemistry. 1997 Sep 16;36(37):11061-8. PMID:9333323
Page seeded by OCA on Tue Oct 30 10:39:09 2007
