1qvs: Difference between revisions

Revision as of 13:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qvs.png

Template:STRUCTURE 1qvs

Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein ACrystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A

Template:ABSTRACT PUBMED 14556621

About this StructureAbout this Structure

1QVS is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Presence of ferric hydroxide clusters in mutants of Haemophilus influenzae ferric ion-binding protein A., Shouldice SR, Skene RJ, Dougan DR, McRee DE, Tari LW, Schryvers AB, Biochemistry. 2003 Oct 21;42(41):11908-14. PMID:14556621

Page seeded by OCA on Mon Jul 28 13:56:52 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qvs.jpg|left|200px]]
+{{Seed}}
+[[Image:1qvs.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qvs|  PDB=1qvs  |  SCENE=  }}
-'''Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A'''
+===Crystal Structure of Haemophilus influenzae H9A mutant Holo Ferric ion-Binding Protein A===
-==Overview==
+<!--
-The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. In this study, we report the crystal structures of two mutant forms of ferric ion-binding protein A (FbpA) from Haemophilus influenzae with bound multinuclear oxo-metal clusters. Crystals of site-directed mutants in the metal or anion binding ligands contain protein in the open conformation, and two mutant FbpAs, H9A and N175L, contain different cluster arrangements in the iron-binding pocket. The iron clusters are anchored by binding to the two tyrosine ligands (Tyr195 and Tyr196) positioned at the vertex of the iron-binding pocket but are not coordinated by the other metal binding ligands. Our results suggest that the metal clusters may have formed in situ, suggesting that the mutant FbpAs may serve as a simple model for protein-mediated mineralization.
+The line below this paragraph, {{ABSTRACT_PUBMED_14556621}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14556621 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14556621}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Tari, L W.]]
 [[Category: Metal binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:45:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:56:52 2008''