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[[Image:1pya.jpg|left|200px]]
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[[Image:1pya.png|left|200px]]


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{{STRUCTURE_1pya|  PDB=1pya  |  SCENE=  }}  
{{STRUCTURE_1pya|  PDB=1pya  |  SCENE=  }}  


'''REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A'''
===REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A===




==Overview==
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The crystal structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a has been refined to an R-value of 0.15 (for the 5.0 to 2.5 A resolution shell) and 0.17 (for the 10.0 to 2.5 A resolution shell). A description of the overall structure is presented, focusing on secondary structure and subunit association. The enzyme is a hexamer of alpha beta subunits. Separate alpha and beta-chains arise from an autocatalytic cleavage reaction between two serine residues, which results in the pyruvoyl cofactor. The central core of the alpha beta subunit is a beta-sandwich which consists of two face-to-face three-stranded antiparallel beta-sheets, flanked by alpha-helices on each side. The beta-sandwich creates a stable fold that allows conformational strain to be introduced across an internal cleavage region between the alpha and beta chains and places the pyruvoyl cofactor in a position for efficient electron withdrawal from the substrate. Three alpha beta subunits are related by a molecular three-fold symmetry axis to form a trimer whose interfaces have complementary surfaces and extensive molecular interactions. Each of the interfaces contains an active site and a solvent channel that leads from the active site to the exterior of the molecule. The trimers are related by a crystallographic two-fold symmetry axis to form the hexamer with an overall dumbbell shape. The interface between trimers has few molecular interactions.
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{{ABSTRACT_PUBMED_8464063}}


==About this Structure==
==About this Structure==
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[[Category: Rozwarski, D A.]]
[[Category: Rozwarski, D A.]]
[[Category: Carboxy-lyase]]
[[Category: Carboxy-lyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:38:13 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:15:01 2008''

Revision as of 09:15, 28 July 2008

File:1pya.png

Template:STRUCTURE 1pya

REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A

Template:ABSTRACT PUBMED 8464063

About this Structure

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

Reference

Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a., Gallagher T, Rozwarski DA, Ernst SR, Hackert ML, J Mol Biol. 1993 Mar 20;230(2):516-28. PMID:8464063

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