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.


2j2z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2j2z.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2j2z.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2j2z| PDB=2j2z | SCENE= }}
{{STRUCTURE_2j2z| PDB=2j2z | SCENE= }}
-
'''X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION'''
+
===X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION===
-
==Overview==
+
<!--
-
P pili are important adhesive fibres that are assembled by the conserved chaperone-usher pathway. During pilus assembly, the subunits are incorporated into the growing fibre by the donor-strand exchange mechanism, whereby the beta-strand of the chaperone, which complements the incomplete immunoglobulin fold of each subunit, is displaced by the amino-terminal extension of an incoming subunit in a zip-in-zip-out exchange process that is initiated at the P5 pocket, an exposed hydrophobic pocket in the groove of the subunit. In vivo, termination of P pilus growth requires a specialized subunit, PapH. Here, we show that PapH is incorporated at the base of the growing pilus, where it is unable to undergo donor-strand exchange. This inability is not due to a stronger PapD-PapH interaction, but to a lack of a P5 initiator pocket in the PapH structure, suggesting that PapH terminates pilus growth because it is lacking the initiation point by which donor-strand exchange proceeds.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17082819}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17082819 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17082819}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Periplasmic]]
[[Category: Periplasmic]]
[[Category: Pilus termination]]
[[Category: Pilus termination]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:15:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:13:34 2008''

Revision as of 02:13, 28 July 2008

Template:STRUCTURE 2j2z

X-RAY STRUCTURE OF THE CHAPERONE PAPD IN COMPLEX WITH THE PILUS TERMINATOR SUBUNIT PAPH AT 2.3 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 17082819

About this Structure

2J2Z is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of P pilus termination in uropathogenic Escherichia coli., Verger D, Miller E, Remaut H, Waksman G, Hultgren S, EMBO Rep. 2006 Dec;7(12):1228-32. Epub 2006 Nov 3. PMID:17082819

Page seeded by OCA on Mon Jul 28 05:13:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools