We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1gvc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gvc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1gvc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gvc| PDB=1gvc | SCENE= }}
{{STRUCTURE_1gvc| PDB=1gvc | SCENE= }}
-
'''18KDA N-II DOMAIN FRAGMENT OF DUCK OVOTRANSFERRIN + NTA'''
+
===18KDA N-II DOMAIN FRAGMENT OF DUCK OVOTRANSFERRIN + NTA===
-
==Overview==
+
<!--
-
In a previous paper [Lindley et al. (1993), Acta Cryst. D49, 292-304], the X-ray structure analysis of the 18 kDa fragment of duck ovotransferrin, corresponding to the NII domain of the intact protein, was reported at a resolution of 2.3 A. In this structure, the Fe(III) cation binds to two tyrosine residues and the synergistic carbonate anion in an identical manner to that found in the intact protein. However, the aspartate and histidine residues, normally involved in iron binding in transferrins, are absent in the fragment and it was not possible to unequivocally define what had replaced them. The electron density was tentatively assigned to be a mixture of peptides, presumably resulting from the proteolytic preparation of the fragment, binding to the iron through their amino and carboxylate termini. A more recent X-ray analysis of the fragment, from a different preparation, has resulted in a structure at 1.95 A, in which glycine appears to be the predominant residue bound to the cation. In an alternative attempt to clarify the binding of iron to the 18 kDa fragment, the metal was removed by dialysis and replaced in the form of ferric nitrilotriacetate. Crystallization of this complex has resulted in an X-ray structure at 1.90 A in which the Fe(III) is bound to the synergistic carbonate anion and only one tyrosine residue in a manner almost identical to the intact protein. The carboxylate groups and the tertiary amino group of the nitrilotriacetate occupy the remaining coordination sites. The second tyrosine residue, Tyr95, is not bound directly to the iron. The implication of these structures with respect to the mechanism of iron binding by the transferrins is addressed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11976488}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11976488 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11976488}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Iron transport]]
[[Category: Iron transport]]
[[Category: Metal-binding]]
[[Category: Metal-binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:03:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:08:35 2008''

Revision as of 03:08, 1 July 2008

Image:1gvc.png

Template:STRUCTURE 1gvc

18KDA N-II DOMAIN FRAGMENT OF DUCK OVOTRANSFERRIN + NTA

Template:ABSTRACT PUBMED 11976488

About this Structure

1GVC is a Single protein structure of sequence from Anas platyrhynchos. Full crystallographic information is available from OCA.

Reference

The mechanism of iron uptake by transferrins: the X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex., Kuser P, Hall DR, Haw ML, Neu M, Evans RW, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):777-83. Epub 2002, Apr 26. PMID:11976488

Page seeded by OCA on Tue Jul 1 06:08:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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