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1xvy

From Proteopedia

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Current revision

Crystal Structure of iron-free Serratia marcescens SfuA

Structural highlights

1xvy is a 1 chain structure with sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.74Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FBPA_SERMA Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (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

The uptake of the element iron is vital for the survival of most organisms. Numerous pathogenic Gram-negative bacteria utilize a periplasm-to-cytosol ATP-binding cassette transport pathway to transport this essential atom in to the cell. In this study, we investigated the Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding periplasmic proteins. We have determined the 1.8-angstroms structures of iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins. Although the sequence of these proteins varies considerably from the other members of the transferrin structural superfamily, they adopt the same three-dimensional fold. The iron-loaded YfuA structure illustrates the unique nature of this new class of proteins in that they are able to octahedrally coordinate the ferric ion in the absence of a bound anion. The iron-free SfuA structure contains a bound citrate anion in the iron-binding cleft that tethers the N- and C-terminal domains of the apo protein and stabilizes the partially open structure.

Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins.,Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB J Biol Chem. 2005 Feb 18;280(7):5820-7. Epub 2004 Dec 2. PMID:15576371^[1]

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

References

↑ Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB. Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins. J Biol Chem. 2005 Feb 18;280(7):5820-7. Epub 2004 Dec 2. PMID:15576371 doi:10.1074/jbc.M411238200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1xvy' size='340' side='right'caption='[[1xvy]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xvy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XVY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xvy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XVY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xvx|1xvx]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sfuA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvy OCA], [https://pdbe.org/1xvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xvy RCSB], [https://www.ebi.ac.uk/pdbsum/1xvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvy ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvy OCA], [http://pdbe.org/1xvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xvy RCSB], [http://www.ebi.ac.uk/pdbsum/1xvy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FBPA_SERMA FBPA_SERMA]] Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (By similarity).
+[https://www.uniprot.org/uniprot/FBPA_SERMA FBPA_SERMA] Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
 [[Category: Large Structures]]
-[[Category: Dougan, D R]]
+[[Category: Yersinia enterocolitica]]
-[[Category: McRee, D E]]
+[[Category: Dougan DR]]
-[[Category: Schryvers, A B]]
+[[Category: McRee DE]]
-[[Category: Shouldice, S R]]
+[[Category: Schryvers AB]]
-[[Category: Tari, L W]]
+[[Category: Shouldice SR]]
-[[Category: Iron binding protein]]
+[[Category: Tari LW]]
-[[Category: Periplasmic iron binding protein]]

1xvy

From Proteopedia

Current revision

Crystal Structure of iron-free Serratia marcescens SfuA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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