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3I6B

Crystal structure of YrbI lacking the last 8 residues, in complex with Kdo and inorganic phosphate

Summary for 3I6B
Entry DOI10.2210/pdb3i6b/pdb
Related2R8E 2R8X 2R8Y 2R8Z 3HYC
Descriptor3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordsyrbi, kdsc, kdo, phosphatase, hydrolase, lipopolysaccharide biosynthesis, magnesium
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight77778.46
Authors
Biswas, T.,Tsodikov, O.V. (deposition date: 2009-07-06, release date: 2009-09-01, Last modification date: 2023-09-06)
Primary citationBiswas, T.,Yi, L.,Aggarwal, P.,Wu, J.,Rubin, J.R.,Stuckey, J.A.,Woodard, R.W.,Tsodikov, O.V.
The Tail of KdsC: CONFORMATIONAL CHANGES CONTROL THE ACTIVITY OF A HALOACID DEHALOGENASE SUPERFAMILY PHOSPHATASE.
J.Biol.Chem., 284:30594-30603, 2009
Cited by
PubMed Abstract: The phosphatase KdsC cleaves 3-deoxy-D-manno-octulosonate 8-phosphate to generate a molecule of inorganic phosphate and Kdo. Kdo is an essential component of the lipopolysaccharide envelope in Gram-negative bacteria. Because lipopolysaccharide is an important determinant of bacterial resistance and toxicity, KdsC is a potential target for novel antibacterial agents. KdsC belongs to the broad haloacid dehalogenase superfamily. In haloacid dehalogenase superfamily enzymes, substrate specificity and catalytic efficiency are generally dictated by a fold feature called the cap domain. It is therefore not clear why KdsC, which lacks a cap domain, is catalytically efficient and highly specific to 3-deoxy-D-manno-octulosonate 8-phosphate. Here, we present a set of seven structures of tetrameric Escherichia coli KdsC (ranging from 1.4 to 3.06 A in resolution) that model different intermediate states in its catalytic mechanism. A crystal structure of product-bound E. coli KdsC shows how the interface between adjacent monomers defines the active site pocket. Kdo is engaged in a network of polar and nonpolar interactions with residues at this interface, which explains substrate specificity. Furthermore, this structural and kinetic analysis strongly suggests that the binding of the flexible C-terminal region (tail) to the active site makes KdsC catalytically efficient by facilitating product release.
PubMed: 19726684
DOI: 10.1074/jbc.M109.012278
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.49 Å)
Structure validation

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