1eq2
From Proteopedia
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|PDB= 1eq2 |SIZE=350|CAPTION= <scene name='initialview01'>1eq2</scene>, resolution 2.0Å | |PDB= 1eq2 |SIZE=350|CAPTION= <scene name='initialview01'>1eq2</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADQ:ADENOSINE-5'-DIPHOSPHATE-GLUCOSE'>ADQ</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ADP-glyceromanno-heptose_6-epimerase ADP-glyceromanno-heptose 6-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.20 5.1.3.20] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-glyceromanno-heptose_6-epimerase ADP-glyceromanno-heptose 6-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.20 5.1.3.20] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq2 OCA], [http://www.ebi.ac.uk/pdbsum/1eq2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eq2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jr., W G.Coleman.]] | [[Category: Jr., W G.Coleman.]] | ||
[[Category: Ni, Y S.]] | [[Category: Ni, Y S.]] | ||
| - | [[Category: ADQ]] | ||
| - | [[Category: NAP]] | ||
[[Category: c-terminal mixed alpha/beta domain]] | [[Category: c-terminal mixed alpha/beta domain]] | ||
[[Category: n-terminal domain rossmann fold]] | [[Category: n-terminal domain rossmann fold]] | ||
[[Category: short-chain dehydrogenase/reductase fold]] | [[Category: short-chain dehydrogenase/reductase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:31 2008'' |
Revision as of 17:07, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | ADP-glyceromanno-heptose 6-epimerase, with EC number 5.1.3.20 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Overview
BACKGROUND: ADP-L-glycero--mannoheptose 6-epimerase (AGME) is required for lipopolysaccharide (LPS) biosynthesis in most genera of pathogenic and non-pathogenic Gram-negative bacteria. It catalyzes the interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose, a precursor of the seven-carbon sugar L-glycero-mannoheptose (heptose). Heptose is an obligatory component of the LPS core domain; its absence results in a truncated LPS structure resulting in susceptibility to hydrophobic antibiotics. Heptose is not found in mammalian cells, thus its biosynthetic pathway in bacteria presents a unique target for the design of novel antimicrobial agents. RESULTS: The structure of AGME, in complex with NADP and the catalytic inhibitor ADP-glucose, has been determined at 2.0 A resolution by multiwavelength anomalous diffraction (MAD) phasing methods. AGME is a homopentameric enzyme, which crystallizes with two pentamers in the asymmetric unit. The location of 70 crystallographically independent selenium sites was a key step in the structure determination process. Each monomer comprises two domains: a large N-terminal domain, consisting of a modified seven-stranded Rossmann fold that is associated with NADP binding; and a smaller alpha/beta C-terminal domain involved in substrate binding. CONCLUSIONS: The first structure of an LPS core biosynthetic enzyme leads to an understanding of the mechanism of the conversion between ADP-D-glycero--mannoheptose and ADP-L-glycero-D-mannoheptose. On the basis of its high structural similarity to UDP-galactose epimerase and the three-dimensional positions of the conserved residues Ser116, Tyr140 and Lys144, AGME was classified as a member of the short-chain dehydrogenase/reductase (SDR) superfamily. This study should prove useful in the design of mechanistic and structure-based inhibitors of the AGME catalyzed reaction.
About this Structure
1EQ2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist., Deacon AM, Ni YS, Coleman WG Jr, Ealick SE, Structure. 2000 May 15;8(5):453-62. PMID:10896473
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