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.

1gv8

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:41, 6 March 2019

18 kDa fragment of N-II domain of duck ovotransferrin

Structural highlights

1gv8 is a 1 chain structure with sequence from Anas platyrhynchos. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1aov, 1dot, 1ovb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRFE_ANAPL] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Ovotransferrin has a bacteriostatic function. Its concentration in avian egg is the highest concentration of any transferrin in vivo (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kuser P, Hall DR, Haw ML, Neu M, Evans RW, Lindley PF. 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. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):777-83. Epub 2002, Apr 26. PMID:11976488

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gv8"

@@ Line 1: / Line 1: @@
 ==18 kDa fragment of N-II domain of duck ovotransferrin==
-<StructureSection load='1gv8' size='340' side='right' caption='[[1gv8]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='1gv8' size='340' side='right'  caption='[[1gv8]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1gv8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GV8 FirstGlance]. <br>
@@ Line 14: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gv8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gv/1gv8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1gv8

From Proteopedia

Revision as of 07:41, 6 March 2019

18 kDa fragment of N-II domain of duck ovotransferrin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox