1s4c
YHCH PROTEIN (HI0227) COPPER COMPLEX
Structural highlights
FunctionNANQ_HAEIN Opens both the alpha- and beta-forms of N-acetylneuraminate (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate for NanA (Probable). Has preferential activity on the beta-anomer rather than the alpha-anomer. Accelerates a reaction that is spontaneous at slightly alkaline pH, facilitates the reaction at acidic pH (By similarity).[UniProtKB:P45424][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid. Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism.,Teplyakov A, Obmolova G, Toedt J, Galperin MY, Gilliland GL J Bacteriol. 2005 Aug;187(16):5520-7. PMID:16077096[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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