2vp1

From Proteopedia

(Difference between revisions)

Current revision

Fe-FutA2 from Synechocystis PCC6803

Structural highlights

2vp1 is a 2 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUTA2_SYNY3 Probably part of a periplasmic ABC transporter complex futA1A2BC (TC 3.A.1.10.2) involved in Fe(3+) ion import (ferric iron). This protein and futA1 (slr1295) are subunit proteins that have redundant or overlapping substrate-binding functions (Probable). The differing subcellular locations of futA1 (predominantly thylakoid lumen) and futA2 (predominantly periplasmic) suggest they may fulfill different roles.^[1] ^[2] Plays an important role in protecting the acceptor side of photosystem II (PSII) against oxidative damage, especially under iron-limiting growth conditions (Potential).^[3] ^[4] Plays an undefined role in copper supply to thylakoid proteins.^[5] ^[6]

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

Synechocystis PCC 6803 has a high demand for iron (10 times greater than Escherichia coli) to sustain photosynthesis and is unusual in possessing at least two putative iron-binding proteins of a type normally associated with ATP-binding cassette-type importers. It has been suggested that one of these, FutA2, binds ferrous iron, but herein we clearly demonstrate that this protein avidly binds Fe(III), the oxidation state preference of periplasmic iron-binding proteins. Structures of apo-FutA2 and Fe-FutA2 have been determined at 1.7 and 2.7A, respectively. The metal ion is bound in a distorted trigonal bipyramidal arrangement with no exogenous anions as ligands. The metal-binding environment, including the second coordination sphere and charge properties, is consistent with a preference for Fe(III). Atypically, FutA2 has a Tat signal peptide, and its inability to coordinate divalent cations may be crucial to prevent metals from binding to the folded protein prior to export from the cytosol. A loop containing the His(43) ligand undergoes considerable movement in apo-versus Fe-FutA2 and may control metal release to the importer. Although these data are consistent with FutA2 being the periplasmic component involved in iron uptake, deletion of another putative ferric binding protein, FutA1, has a greater effect on the accumulation of iron and is more analogous to a DeltafutA1DeltafutA2 double mutant than DeltafutA2. Here, we also discover that there is a reduced level of ferric FutA2 in the periplasm of the DeltafutA1 mutant providing an explanation for its severe iron-uptake phenotype.

FutA2 is a ferric binding protein from Synechocystis PCC 6803.,Badarau A, Firbank SJ, Waldron KJ, Yanagisawa S, Robinson NJ, Banfield MJ, Dennison C J Biol Chem. 2008 May 2;283(18):12520-7. Epub 2008 Feb 4. PMID:18252722^[7]

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

References

↑ Katoh H, Hagino N, Grossman AR, Ogawa T. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol. 2001 May;183(9):2779-84. PMID:11292796 doi:http://dx.doi.org/10.1128/JB.183.9.2779-2784.2001
↑ Waldron KJ, Tottey S, Yanagisawa S, Dennison C, Robinson NJ. A periplasmic iron-binding protein contributes toward inward copper supply. J Biol Chem. 2007 Feb 9;282(6):3837-46. Epub 2006 Dec 5. PMID:17148438 doi:http://dx.doi.org/M609916200
↑ Katoh H, Hagino N, Grossman AR, Ogawa T. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol. 2001 May;183(9):2779-84. PMID:11292796 doi:http://dx.doi.org/10.1128/JB.183.9.2779-2784.2001
↑ Waldron KJ, Tottey S, Yanagisawa S, Dennison C, Robinson NJ. A periplasmic iron-binding protein contributes toward inward copper supply. J Biol Chem. 2007 Feb 9;282(6):3837-46. Epub 2006 Dec 5. PMID:17148438 doi:http://dx.doi.org/M609916200
↑ Katoh H, Hagino N, Grossman AR, Ogawa T. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol. 2001 May;183(9):2779-84. PMID:11292796 doi:http://dx.doi.org/10.1128/JB.183.9.2779-2784.2001
↑ Waldron KJ, Tottey S, Yanagisawa S, Dennison C, Robinson NJ. A periplasmic iron-binding protein contributes toward inward copper supply. J Biol Chem. 2007 Feb 9;282(6):3837-46. Epub 2006 Dec 5. PMID:17148438 doi:http://dx.doi.org/M609916200
↑ Badarau A, Firbank SJ, Waldron KJ, Yanagisawa S, Robinson NJ, Banfield MJ, Dennison C. FutA2 is a ferric binding protein from Synechocystis PCC 6803. J Biol Chem. 2008 May 2;283(18):12520-7. Epub 2008 Feb 4. PMID:18252722 doi:http://dx.doi.org/10.1074/jbc.M709907200

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/2vp1"

@@ Line 1: / Line 1: @@
-[[Image:2vp1.png|left|200px]]
-{{STRUCTURE_2vp1|  PDB=2vp1  |  SCENE=  }}
+==Fe-FutA2 from Synechocystis PCC6803==
+<StructureSection load='2vp1' size='340' side='right'caption='[[2vp1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2vp1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VP1 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=2vp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vp1 OCA], [https://pdbe.org/2vp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vp1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vp1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUTA2_SYNY3 FUTA2_SYNY3] Probably part of a periplasmic ABC transporter complex futA1A2BC (TC 3.A.1.10.2) involved in Fe(3+) ion import (ferric iron). This protein and futA1 (slr1295) are subunit proteins that have redundant or overlapping substrate-binding functions (Probable). The differing subcellular locations of futA1 (predominantly thylakoid lumen) and futA2 (predominantly periplasmic) suggest they may fulfill different roles.<ref>PMID:11292796</ref> <ref>PMID:17148438</ref>   Plays an important role in protecting the acceptor side of photosystem II (PSII) against oxidative damage, especially under iron-limiting growth conditions (Potential).<ref>PMID:11292796</ref> <ref>PMID:17148438</ref>   Plays an undefined role in copper supply to thylakoid proteins.<ref>PMID:11292796</ref> <ref>PMID:17148438</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vp/2vp1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vp1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Synechocystis PCC 6803 has a high demand for iron (10 times greater than Escherichia coli) to sustain photosynthesis and is unusual in possessing at least two putative iron-binding proteins of a type normally associated with ATP-binding cassette-type importers. It has been suggested that one of these, FutA2, binds ferrous iron, but herein we clearly demonstrate that this protein avidly binds Fe(III), the oxidation state preference of periplasmic iron-binding proteins. Structures of apo-FutA2 and Fe-FutA2 have been determined at 1.7 and 2.7A, respectively. The metal ion is bound in a distorted trigonal bipyramidal arrangement with no exogenous anions as ligands. The metal-binding environment, including the second coordination sphere and charge properties, is consistent with a preference for Fe(III). Atypically, FutA2 has a Tat signal peptide, and its inability to coordinate divalent cations may be crucial to prevent metals from binding to the folded protein prior to export from the cytosol. A loop containing the His(43) ligand undergoes considerable movement in apo-versus Fe-FutA2 and may control metal release to the importer. Although these data are consistent with FutA2 being the periplasmic component involved in iron uptake, deletion of another putative ferric binding protein, FutA1, has a greater effect on the accumulation of iron and is more analogous to a DeltafutA1DeltafutA2 double mutant than DeltafutA2. Here, we also discover that there is a reduced level of ferric FutA2 in the periplasm of the DeltafutA1 mutant providing an explanation for its severe iron-uptake phenotype.
-===FE-FUTA2 FROM SYNECHOCYSTIS PCC6803===
+FutA2 is a ferric binding protein from Synechocystis PCC 6803.,Badarau A, Firbank SJ, Waldron KJ, Yanagisawa S, Robinson NJ, Banfield MJ, Dennison C J Biol Chem. 2008 May 2;283(18):12520-7. Epub 2008 Feb 4. PMID:18252722<ref>PMID:18252722</ref>
-{{ABSTRACT_PUBMED_18252722}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2vp1" style="background-color:#fffaf0;"></div>
-[[2vp1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VP1 OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:018252722</ref><references group="xtra"/>
+</StructureSection>
-[[Category: Synechocystis sp.]]
+[[Category: Large Structures]]
-[[Category: Badarau, A.]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Banfield, M J.]]
+[[Category: Badarau A]]
-[[Category: Dennison, C.]]
+[[Category: Banfield MJ]]
-[[Category: Firbank, S J.]]
+[[Category: Dennison C]]
-[[Category: Ferric binding protein]]
+[[Category: Firbank SJ]]
-[[Category: Futa2]]
-[[Category: Iron]]
-[[Category: Metal-binding protein]]
-[[Category: Synechocysti]]
-[[Category: Tat]]

2vp1

From Proteopedia

Current revision

Fe-FutA2 from Synechocystis PCC6803

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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