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| - | [[Image:1pya.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1pya| PDB=1pya | SCENE= }} | | {{STRUCTURE_1pya| PDB=1pya | SCENE= }} |
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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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| - | ==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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8464063}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8464063 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8464063}} |
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| | ==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
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
Page seeded by OCA on Mon Jul 28 12:15:01 2008
