1HQ6
STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8
Summary for 1HQ6
| Entry DOI | 10.2210/pdb1hq6/pdb |
| Related | 1PYA |
| Descriptor | HISTIDINE DECARBOXYLASE (3 entities in total) |
| Functional Keywords | helix disorder, ph regulation, less active form, pyruvoyl, carboxy-lyase, lyase |
| Biological source | Lactobacillus sp. More |
| Total number of polymer chains | 4 |
| Total formula weight | 68272.41 |
| Authors | Schelp, E.,Worley, S.,Monzingo, A.F.,Ernst, S.,Robertus, J.D. (deposition date: 2000-12-14, release date: 2001-03-21, Last modification date: 2024-11-20) |
| Primary citation | Schelp, E.,Worley, S.,Monzingo, A.F.,Ernst, S.,Robertus, J.D. pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. J.Mol.Biol., 306:727-732, 2001 Cited by PubMed Abstract: 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. PubMed: 11243783DOI: 10.1006/jmbi.2000.4430 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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