1pya

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[[Image:1pya.jpg|left|200px]]
[[Image:1pya.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1pya |SIZE=350|CAPTION= <scene name='initialview01'>1pya</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1pya", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_decarboxylase Histidine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.22 4.1.1.22] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1pya| PDB=1pya | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pya OCA], [http://www.ebi.ac.uk/pdbsum/1pya PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pya RCSB]</span>
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}}
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'''REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A'''
'''REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A'''
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[[Category: Hackert, M L.]]
[[Category: Hackert, M L.]]
[[Category: Rozwarski, D A.]]
[[Category: Rozwarski, D A.]]
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[[Category: carboxy-lyase]]
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[[Category: Carboxy-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:38:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:11 2008''
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Revision as of 02:38, 3 May 2008

Image:1pya.jpg

Template:STRUCTURE 1pya

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


Overview

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.

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 Page seeded by OCA on Sat May 3 05:38:13 2008

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