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.


1e5l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1e5l.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1e5l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e5l| PDB=1e5l | SCENE= }}
{{STRUCTURE_1e5l| PDB=1e5l | SCENE= }}
-
'''APO SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA'''
+
===APO SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA===
-
==Overview==
+
<!--
-
BACKGROUND: The biosynthesis of the essential amino acid lysine in higher fungi and cyanobacteria occurs via the alpha-aminoadipate pathway, which is completely different from the lysine biosynthetic pathway found in plants and bacteria. The penultimate reaction in the alpha-aminoadipate pathway is catalysed by NADPH-dependent saccharopine reductase. We set out to determine the structure of this enzyme as a first step in exploring the structural biology of fungal lysine biosynthesis. RESULTS: We have determined the three-dimensional structure of saccharopine reductase from the plant pathogen Magnaporthe grisea in its apo form to 2.0 A resolution and as a ternary complex with NADPH and saccharopine to 2.1 A resolution. Saccharopine reductase is a homodimer, and each subunit consists of three domains, which are not consecutive in amino acid sequence. Domain I contains a variant of the Rossmann fold that binds NADPH. Domain II folds into a mixed seven-stranded beta sheet flanked by alpha helices and is involved in substrate binding and dimer formation. Domain III is all-helical. The structure analysis of the ternary complex reveals a large movement of domain III upon ligand binding. The active site is positioned in a cleft between the NADPH-binding domain and the second alpha/beta domain. Saccharopine is tightly bound to the enzyme via a number of hydrogen bonds to invariant amino acid residues. CONCLUSIONS: On the basis of the structure of the ternary complex of saccharopine reductase, an enzymatic mechanism is proposed that includes the formation of a Schiff base as a key intermediate. Despite the lack of overall sequence homology, the fold of saccharopine reductase is similar to that observed in some enzymes of the diaminopimelate pathway of lysine biosynthesis in bacteria. These structural similarities suggest an evolutionary relationship between two different major families of amino acid biosynthetic pathway, the glutamate and aspartate families.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11080625}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11080625 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11080625}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Lysine biosynthesis]]
[[Category: Lysine biosynthesis]]
[[Category: Saccharopine reductase]]
[[Category: Saccharopine reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:41:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:11:16 2008''

Revision as of 21:11, 30 June 2008

Image:1e5l.png

Template:STRUCTURE 1e5l

APO SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA

Template:ABSTRACT PUBMED 11080625

About this Structure

1E5L is a Single protein structure of sequence from Magnaporthe grisea. Full crystallographic information is available from OCA.

Reference

Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis., Johansson E, Steffens JJ, Lindqvist Y, Schneider G, Structure. 2000 Oct 15;8(10):1037-47. PMID:11080625

Page seeded by OCA on Tue Jul 1 00:11:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e5l"
Personal tools