1pya
From Proteopedia
(New page: 200px<br /><applet load="1pya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pya, resolution 2.5Å" /> '''REFINED STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1pya.jpg|left|200px]]<br /><applet load="1pya" size=" | + | [[Image:1pya.jpg|left|200px]]<br /><applet load="1pya" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pya, resolution 2.5Å" /> | caption="1pya, resolution 2.5Å" /> | ||
'''REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A'''<br /> | '''REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the pyruvoyl-dependent histidine decarboxylase | + | 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== | ==About this Structure== | ||
| - | 1PYA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Active as [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] Full crystallographic information is available from [http:// | + | 1PYA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYA OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Lactobacillus sp.]] | [[Category: Lactobacillus sp.]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Ernst, S | + | [[Category: Ernst, S R.]] |
[[Category: Gallagher, T.]] | [[Category: Gallagher, T.]] | ||
| - | [[Category: Hackert, M | + | [[Category: Hackert, M L.]] |
| - | [[Category: Rozwarski, D | + | [[Category: Rozwarski, D A.]] |
[[Category: carboxy-lyase]] | [[Category: carboxy-lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:49 2008'' |
Revision as of 12:33, 21 February 2008
|
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.. Active as Histidine decarboxylase, with EC number 4.1.1.22 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 Thu Feb 21 14:33:49 2008
