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.


1ysc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ysc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ysc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ysc| PDB=1ysc | SCENE= }}
{{STRUCTURE_1ysc| PDB=1ysc | SCENE= }}
-
'''2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE'''
+
===2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE===
-
==Overview==
+
<!--
-
The structure of monomeric serine carboxypeptidase from Saccharomyces cerevisiae (CPD-Y), deglycosylated by an efficient new procedure, has been determined by multiple isomorphous replacement and crystallographic refinement. The model contains 3333 non-hydrogen atoms, all 421 amino acids, 3 of 4 carbohydrate residues, 5 disulfide bridges, and 38 water molecules. The standard crystallographic R-factor is 0.162 for 10,909 reflections observed between 20.0- and 2.8-A resolution. The model has rms deviations from ideality of 0.016 A for bond lengths and 2.7 degrees for bond angles and from restrained thermal parameters of 7.9 A2. CPD-Y, which exhibits a preference for hydrophobic peptides, is distantly related to dimeric wheat serine carboxypeptidase II (CPD-WII), which has a preference for basic peptides. Comparison of the two structures suggests that substitution of hydrophobic residues in CPD-Y for negatively charged residues in CPD-WII in the binding site is largely responsible for this difference. Catalytic residues are in essentially identical configurations in the two molecules, including strained main-chain conformational angles for three active site residues (Ser 146, Gly 52, and Gly 53) and an unusual hydrogen bond between the carboxyl groups of Glu 145 and Glu 65. The binding of an inhibitor, benzylsuccinic acid, suggests that the C-terminal carboxylate binding site for peptide substrates is Asn 51, Gly 52, Glu 145, and His 397 and that the "oxyanion hole" consists of the amides of Gly 53 and Tyr 147. A surprising result of the study is that the domains consisting of residues 180-317, which form a largely alpha-helical insertion into the highly conserved cores surrounding the active site, are quite different structurally in the two molecules. It is suggested that these domains have evolved much more rapidly than other parts of the molecule and are involved in substrate recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7727362}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7727362 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7727362}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Endrizzi, J A.]]
[[Category: Endrizzi, J A.]]
[[Category: Remington, S J.]]
[[Category: Remington, S J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:43:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:12:32 2008''

Revision as of 14:12, 27 July 2008

Image:1ysc.png

Template:STRUCTURE 1ysc

2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE

Template:ABSTRACT PUBMED 7727362

About this Structure

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

Reference

2.8-A structure of yeast serine carboxypeptidase., Endrizzi JA, Breddam K, Remington SJ, Biochemistry. 1994 Sep 20;33(37):11106-20. PMID:7727362

Page seeded by OCA on Sun Jul 27 17:12:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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