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.


2o69

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o69.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2o69.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o69| PDB=2o69 | SCENE= }}
{{STRUCTURE_2o69| PDB=2o69 | SCENE= }}
-
'''Crystal Structure of Haemophilus influenzae N193L mutant FbpA'''
+
===Crystal Structure of Haemophilus influenzae N193L mutant FbpA===
-
==Overview==
+
<!--
-
The acquisition of iron from transferrin by Gram-negative bacterial pathogens is dependent on a periplasmic ferric-ion-binding protein, FbpA. FbpA shuttles iron from the outer membrane to an inner membrane transport complex. A bound phosphate anion completes the iron co-ordination shell of FbpA and kinetic studies demonstrate that the anion plays a critical role in iron binding and release in vitro. The present study was initiated to directly address the hypothesis that the synergistic anion is required for transport of iron in intact cells. A series of site-directed mutants in the anion-binding amino acids of the Haemophilus influenzae FbpA (Gln-58, Asn-175 and Asn-193) were prepared to provide proteins defective in binding of the phosphate anion. Crystal structures of various mutants have revealed that alteration of the C-terminal domain ligands (Asn-175 or Asn-193) but not the N-terminal domain ligand (Gln-58) abrogated binding of the phosphate anion. The mutant proteins were introduced into H. influenzae to evaluate their ability to mediate iron transport. All of the single site-directed mutants (Q58L, N175L and N193L) were capable of mediating iron acquisition from transferrin and from limiting concentrations of ferric citrate. The results suggest that the transport of iron by FbpA is not dependent on binding of phosphate in the synergistic anion-binding site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17147516}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17147516 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17147516}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Metal binding protein]]
[[Category: Metal binding protein]]
[[Category: Mixed beta sheet]]
[[Category: Mixed beta sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 5 10:08:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:49:06 2008''

Revision as of 03:49, 29 July 2008

Image:2o69.png

Template:STRUCTURE 2o69

Crystal Structure of Haemophilus influenzae N193L mutant FbpA

Template:ABSTRACT PUBMED 17147516

About this Structure

2O69 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

The role of the synergistic phosphate anion in iron transport by the periplasmic iron-binding protein from Haemophilus influenzae., Khan AG, Shouldice SR, Tari LW, Schryvers AB, Biochem J. 2007 Apr 1;403(1):43-8. PMID:17147516

Page seeded by OCA on Tue Jul 29 06:49:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o69"
Personal tools