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.


1zde

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zde.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zde.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zde| PDB=1zde | SCENE= }}
{{STRUCTURE_1zde| PDB=1zde | SCENE= }}
-
'''1.95 Angstrom Crystal Structure of a dnaE Intein Precursor from Synechocystis Sp. Pcc 6803'''
+
===1.95 Angstrom Crystal Structure of a dnaE Intein Precursor from Synechocystis Sp. Pcc 6803===
-
==Overview==
+
<!--
-
The first naturally occurring split intein was found in the dnaE gene of Synechocystis sp. PCC6803 and belongs to a subclass of inteins without a penultimate histidine residue. We describe two high-resolution crystal structures, one derived from an excised Ssp DnaE intein and the second from a splicing-deficient precursor protein. The X-ray structures indicate that His147 in the conserved block F activates the side-chain N(delta) atom of the intein C-terminal Asn159, leading to a nucleophilic attack on the peptide bond carbonyl carbon atom at the C-terminal splice site. In this process, Arg73 appears to stabilize the transition state by interacting with the carbonyl oxygen atom of the scissile bond. Arg73 also seems to substitute for the conserved penultimate histidine residue in the formation of an oxyanion hole, as previously identified in other inteins. The finding that the precursor structure contains a zinc ion chelating the highly conserved Cys160 and Asp140 reveals the structural basis of Zn2+-mediated inhibition of protein splicing. Furthermore, it is of interest to observe that the carbonyl carbon atom of Asn159 and N(eta) of Arg73 are 2.6 angstroms apart in the free intein structure and 10.6 angstroms apart in the precursor structure. The orientation change of the aromatic ring of Tyr-1 following the initial acyl shift may be a key switching event contributing to the alignment of Arg73 and the C-terminal scissile bond, and may explain the sequential reaction property of the Ssp DnaE intein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16219320}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16219320 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16219320}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Precursor]]
[[Category: Precursor]]
[[Category: Splicing]]
[[Category: Splicing]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:29:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:30:40 2008''

Revision as of 00:30, 28 July 2008

Image:1zde.png

Template:STRUCTURE 1zde

1.95 Angstrom Crystal Structure of a dnaE Intein Precursor from Synechocystis Sp. Pcc 6803

Template:ABSTRACT PUBMED 16219320

About this Structure

1ZDE is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

Crystal structures of an intein from the split dnaE gene of Synechocystis sp. PCC6803 reveal the catalytic model without the penultimate histidine and the mechanism of zinc ion inhibition of protein splicing., Sun P, Ye S, Ferrandon S, Evans TC, Xu MQ, Rao Z, J Mol Biol. 2005 Nov 11;353(5):1093-105. Epub 2005 Sep 30. PMID:16219320

Page seeded by OCA on Mon Jul 28 03:30:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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