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.


1n8p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1n8p.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1n8p.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n8p| PDB=1n8p | SCENE= }}
{{STRUCTURE_1n8p| PDB=1n8p | SCENE= }}
-
'''Crystal Structure of cystathionine gamma-lyase from yeast'''
+
===Crystal Structure of cystathionine gamma-lyase from yeast===
-
==Overview==
+
<!--
-
The crystal structure of cystathionine gamma-lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 A. The molecule consists of 393 amino acid residues and one PLP moiety and is arranged in the crystal as a tetramer with D2 symmetry as in other related enzymes of the Cys-Met-metabolism PLP-dependent family like cystathionine beta-lyase (CBL). A structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity between the different family members. CGLs from yeast or human are virtually identical at their active sites to cystathionine gamma-synthase (CGS) from E. coli. Both CGLs and bacterial CGSs exhibit gamma-synthase and gamma-lyase activities depending on their position in the metabolic pathway and the available substrates. This group of enzymes has a glutamate (E333 in yeast CGL) which binds to the distal group of cystathionine (CTT) or the amino group of cysteine. Plant CGSs use homoserine phosphate instead of O-succinyl-homoserine as one substrate. This is reflected by a partially different active site structure in plant CGSs. In CGL and CBL the pseudosymmetric substrate must dock at the active site in different orientations, with S in gamma-position (CBL) or in delta-position (CGL). The conserved glutamate steers the substrate as seen in other CGLs. In CBLs this position is occupied by either tyrosine or hydrophobic residues directing binding of CTT such that S is in the in gamma-position. In methionine gamma-lyase a hydrophic patch operates as recognition site for the methyl group of the methionine substrate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12715888}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12715888 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12715888}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Worbs, M.]]
[[Category: Worbs, M.]]
[[Category: Three open alpha/beta structure]]
[[Category: Three open alpha/beta structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:13:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:31:08 2008''

Revision as of 06:31, 28 July 2008

Image:1n8p.png

Template:STRUCTURE 1n8p

Crystal Structure of cystathionine gamma-lyase from yeast

Template:ABSTRACT PUBMED 12715888

About this Structure

1N8P is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison., Messerschmidt A, Worbs M, Steegborn C, Wahl MC, Huber R, Laber B, Clausen T, Biol Chem. 2003 Mar;384(3):373-86. PMID:12715888

Page seeded by OCA on Mon Jul 28 09:31:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n8p"
Personal tools