1ibt: Difference between revisions

Revision as of 10:43, 1 July 2008

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File:1ibt.png

Template:STRUCTURE 1ibt

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 CSTRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C

Template:ABSTRACT PUBMED 11835507

About this StructureAbout this Structure

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

ReferenceReference

Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a., Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD, Proteins. 2002 Feb 15;46(3):321-9. PMID:11835507

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-'''STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C'''
+===STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT-170 C===
-==Overview==
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-Histidine decarboxylase (HDC) from Lactobacillus 30a converts histidine to histamine, a process that enables the bacteria to maintain the optimum pH range for cell growth. HDC is regulated by pH; it is active at low pH and inactive at neutral to alkaline pH. The X-ray structure of HDC at pH 8 revealed that a helix was disordered, resulting in the disruption of the substrate-binding site. The HDC trimer has also been shown to exhibit cooperative kinetics at neutral pH, that is, histidine can trigger a T-state to R-state transition. The D53,54N mutant of HDC has an elevated Km, even at low pH, indicating that the enzyme assumes the low activity T-state. We have solved the structures of the D53,54N mutant at low pH, with and without the substrate analog histidine methyl ester (HME) bound. Structural analysis shows that the apo-D53,54N mutant is in the inactive or T-state and that binding of the substrate analog induces the enzyme to adopt the active or R-state. A mechanism for the cooperative transition is proposed.
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 [[Category: Pyruvoyl]]
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