1hq6

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{{STRUCTURE_1hq6| PDB=1hq6 | SCENE= }}
{{STRUCTURE_1hq6| PDB=1hq6 | SCENE= }}
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'''STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8'''
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===STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11243783 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11243783}}
==About this Structure==
==About this Structure==
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[[Category: Ph regulation]]
[[Category: Ph regulation]]
[[Category: Pyruvoyl]]
[[Category: Pyruvoyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:06:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:31:43 2008''

Revision as of 05:31, 1 July 2008

Image:1hq6.png

Template:STRUCTURE 1hq6

STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8

Template:ABSTRACT PUBMED 11243783

About this Structure

1HQ6 is a Protein complex structure of sequences from Lactobacillus sp.. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 1 08:31:43 2008

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