1gq9
From Proteopedia
(New page: 200px<br /> <applet load="1gq9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gq9, resolution 2.6Å" /> '''THE STRUCTURE OF CMP...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1GQ9 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 MG and CTP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GQ9 OCA]]. | + | 1GQ9 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 MG and CTP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38]]. Structure known Active Site: CTA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GQ9 OCA]]. |
==Reference== | ==Reference== | ||
Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product., Jelakovic S, Schulz GE, Biochemistry. 2002 Jan 29;41(4):1174-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11802716 11802716] | Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product., Jelakovic S, Schulz GE, Biochemistry. 2002 Jan 29;41(4):1174-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11802716 11802716] | ||
| + | [[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 24: | Line 25: | ||
[[Category: sugar-activating enzymes]] | [[Category: sugar-activating enzymes]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:31:02 2007'' |
Revision as of 12:26, 30 October 2007
|
THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE COMPLEXED WITH CTP AT 100K
Overview
The activation of the sugar 2-keto-3-deoxy-manno-octonic acid (Kdo) is, catalyzed by CMP-Kdo synthetase (EC 2.7.7.38) and results in a, monophosphate diester with CMP. The enzyme is a pharmaceutical target, because CMP-Kdo is required for the biosynthesis of lipopolysaccharides, that are vital for Gram-negative bacteria. We have established the, structures of an enzyme complex with the educt CTP and of a complex with, the product CMP-Kdo by X-ray diffraction analyses at 100 K, both at 2.6 A, resolution. The N-terminal domains of the dimeric enzyme bind CTP in a, peculiar nucleotide-binding fold with the beta- and gamma-phosphates, located at the so-called "PP-loop", whereas the C-terminal domains, participate in Kdo binding and in the dimer interface. The unstable, nucleotide-sugar ... [(full description)]
About this Structure
1GQ9 is a [Single protein] structure of sequence from [Escherichia coli] with MG and CTP as [ligands]. Active as [3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [2.7.7.38]. Structure known Active Site: CTA. Full crystallographic information is available from [OCA].
Reference
Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product., Jelakovic S, Schulz GE, Biochemistry. 2002 Jan 29;41(4):1174-81. PMID:11802716
Page seeded by OCA on Tue Oct 30 14:31:02 2007
