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.


1f8s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f8s.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f8s.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f8s| PDB=1f8s | SCENE= }}
{{STRUCTURE_1f8s| PDB=1f8s | SCENE= }}
-
'''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.'''
+
===CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.===
-
==Overview==
+
<!--
-
The structure of L-amino acid oxidase (LAAO) from Calloselasma rhodostoma has been determined to 2.0 A resolution in the presence of two ligands: citrate and o-aminobenzoate (AB). The protomer consists of three domains: an FAD-binding domain, a substrate-binding domain and a helical domain. The interface between the substrate-binding and helical domains forms a 25 A long funnel, which provides access to the active site. Three AB molecules are visible within the funnel of the LAAO-AB complex; their orientations suggest the trajectory of the substrate to the active site. The innermost AB molecule makes hydrogen bond contacts with the active site residues, Arg90 and Gly464, and the aromatic portion of the ligand is situated in a hydrophobic pocket. These contacts are proposed to mimic those of the natural substrate. Comparison of LAAO with the structure of mammalian D-amino acid oxidase reveals significant differences in their modes of substrate entry. Furthermore, a mirror-symmetrical relationship between the two substrate-binding sites is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the atoms involved in catalysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10944103}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10944103 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10944103}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: O-aminobenzoate]]
[[Category: O-aminobenzoate]]
[[Category: Oxidase]]
[[Category: Oxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:02:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:52:41 2008''

Revision as of 23:52, 30 June 2008

Image:1f8s.png

Template:STRUCTURE 1f8s

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.

Template:ABSTRACT PUBMED 10944103

About this Structure

1F8S is a Single protein structure of sequence from Calloselasma rhodostoma. Full crystallographic information is available from OCA.

Reference

The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site., Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A, EMBO J. 2000 Aug 15;19(16):4204-15. PMID:10944103

Page seeded by OCA on Tue Jul 1 02:52:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f8s"
Personal tools