1h7f
From Proteopedia
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| - | [[Image:1h7f.gif|left|200px]]<br /><applet load="1h7f" size=" | + | [[Image:1h7f.gif|left|200px]]<br /><applet load="1h7f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h7f, resolution 2.12Å" /> | caption="1h7f, resolution 2.12Å" /> | ||
'''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CMP COMPLEX'''<br /> | '''THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CMP COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H7F 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 C5P as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:C5p Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1H7F 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=C5P:'>C5P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=AC1:C5p+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sugar-activating enzymes]] | [[Category: sugar-activating enzymes]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:20 2008'' |
Revision as of 07:47, 3 February 2008
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THE STRUCTURE OF CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE AND OF ITS COMPLEXES WITH SUBSTRATES AND SUBSTRATE ANALOGUES, CMP COMPLEX
Overview
The enzyme CMP-Kdo synthetase (CKS) catalyzes the activation of the sugar, Kdo (2-keto-3-deoxy-manno-octonic acid) by forming a monophosphate, diester. CKS is a pharmaceutical target because CMP-Kdo is used in the, biosynthesis of lipopolysaccharides that are vital for Gram-negative, bacteria. We have refined the structure of the unligated capsule-specific, CKS from Escherichia coli at 1.8 A resolution (1 A=0.1 nm) and we have, established the structures of its complexes with the substrate CTP, with, CDP and CMP as well as with the product analog CMP-NeuAc (CMP-sialate) by, X-ray diffraction analyses at resolutions between 2.1 A and 2.5 A. The, N-terminal domains of the dimeric enzyme bind CTP in a peculiar, nucleotide-binding fold, whereas the C-terminal domains form the dimer, interface. The observed binding geometries together with the amino acid, variabilities during evolution and the locations of a putative Mg(2+) and, of a very strongly bound water molecule suggest a pathway for the, catalysis. The N-terminal domain shows sequence homology with the, CMP-NeuAc synthetases. Moreover, the chain fold and the substrate-binding, position of CKS resemble those of other enzymes processing, nucleotide-sugars.
About this Structure
1H7F is a Single protein structure of sequence from Escherichia coli with as ligand. Active as 3-deoxy-manno-octulosonate cytidylyltransferase, with EC number 2.7.7.38 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structure of CMP:2-keto-3-deoxy-manno-octonic acid synthetase and of its complexes with substrates and substrate analogs., Jelakovic S, Schulz GE, J Mol Biol. 2001 Sep 7;312(1):143-55. PMID:11545592
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