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| | {{STRUCTURE_1eq2| PDB=1eq2 | SCENE= }} | | {{STRUCTURE_1eq2| PDB=1eq2 | SCENE= }} |
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| - | '''THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE'''
| + | ===THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10896473}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10896473 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10896473}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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 Fri May 2 15:23:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:37:32 2008'' |
Revision as of 22:37, 30 June 2008
Template:STRUCTURE 1eq2
THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Template:ABSTRACT PUBMED 10896473
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
Page seeded by OCA on Tue Jul 1 01:37:32 2008
