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.


2cn4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 29: Line 29:
[[Category: transport protein]]
[[Category: transport protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:08:44 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:13:08 2007''

Revision as of 15:08, 30 October 2007


2cn4, resolution 2.30Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF THE SECRETED DIMERIC FORM OF THE HEMOPHORE HASA REVEALS A DOMAIN SWAPPING WITH AN EXCHANGED HEME LIGAND

Overview

To satisfy their iron needs, several Gram-negative bacteria use a heme, uptake system involving an extracellular heme-binding protein called, hemophore. The function of the hemophore is to acquire free or, hemoprotein-bound heme and to transfer it to HasR, its specific outer, membrane receptor, by protein-protein interaction. The hemophore HasA, secreted by Serratia marcescens, an opportunistic pathogen, was the first, to be identified and is now very well characterized. HasA is a monomer, that binds one b heme with strong affinity. The heme in HasA is highly, exposed to solvent and coordinated by an unusual pair of ligands, a, histidine and a tyrosine. Here, we report the identification, the, characterization and the X-ray structure of a dimeric form of HasA from S., marcescens: DHasA. ... [(full description)]

About this Structure

2CN4 is a [Single protein] structure of sequence from [Serratia marcescens] with PO4 and HEM as [ligands]. Structure known Active Site: HEM. Full crystallographic information is available from [OCA].

Reference

The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand., Czjzek M, Letoffe S, Wandersman C, Delepierre M, Lecroisey A, Izadi-Pruneyre N, J Mol Biol. 2007 Jan 26;365(4):1176-86. Epub 2006 Oct 25. PMID:17113104

Page seeded by OCA on Tue Oct 30 17:13:08 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools