This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1pya

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pya.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1pya.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{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==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_8464063}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools