1hq6

STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8

spinqualitylabelsall models 1hq6, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hq6 is a 4 chain structure with sequence from Lactobacillus sp. 30A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: PYR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DCHS_LACS3 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 PubMed Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure. pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.,Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD J Mol Biol. 2001 Mar 2;306(4):727-32. PMID:11243783 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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