1n4a: Difference between revisions

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<StructureSection load='1n4a' size='340' side='right'caption='[[1n4a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1n4a' size='340' side='right'caption='[[1n4a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1n4a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1n4a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNC:CO-CYANOCOBALAMIN'>CNC</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]] 2&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNC:CO-CYANOCOBALAMIN'>CNC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1efd|1efd]], [[1bmt|1bmt]], [[1n4d|1n4d]]</div></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=1n4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4a OCA], [https://pdbe.org/1n4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4a RCSB], [https://www.ebi.ac.uk/pdbsum/1n4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4a ProSAT], [https://www.topsan.org/Proteins/NESGC/1n4a TOPSAN]</span></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=1n4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4a OCA], [https://pdbe.org/1n4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4a RCSB], [https://www.ebi.ac.uk/pdbsum/1n4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4a ProSAT], [https://www.topsan.org/Proteins/NESGC/1n4a TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BTUF_ECOLI BTUF_ECOLI]] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.<ref>PMID:11790740</ref>
[https://www.uniprot.org/uniprot/BTUF_ECOLI BTUF_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.<ref>PMID:11790740</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1n4a ConSurf].
</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=1n4a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BtuF is the periplasmic binding protein (PBP) for the vitamin B12 transporter BtuCD, a member of the ATP-binding cassette (ABC) transporter superfamily of transmembrane pumps. We have determined crystal structures of Escherichia coli BtuF in the apo state at 3.0 A resolution and with vitamin B12 bound at 2.0 A resolution. The structure of BtuF is similar to that of the FhuD and TroA PBPs and is composed of two alpha/beta domains linked by a rigid alpha-helix. B12 is bound in the "base-on" or vitamin conformation in a wide acidic cleft located between these domains. The C-terminal domain shares structural homology to a B12-binding domain found in a variety of enzymes. The same surface of this domain interacts with opposite surfaces of B12 when comparing ligand-bound structures of BtuF and the homologous enzymes, a change that is probably caused by the obstruction of the face that typically interacts with this domain by the base-on conformation of vitamin B12 bound to BtuF. There is no apparent pseudo-symmetry in the surface properties of the BtuF domains flanking its B12 binding site even though the presumed transport site in the previously reported crystal structure of BtuCD is located in an intersubunit interface with 2-fold symmetry. Unwinding of an alpha-helix in the C-terminal domain of BtuF appears to be part of conformational change involving a general increase in the mobility of this domain in the apo structure compared with the B12-bound structure. As this helix is located on the surface likely to interact with BtuC, unwinding of the helix upon binding to BtuC could play a role in triggering release of B12 into the transport cavity. Furthermore, the high mobility of this domain in free BtuF could provide an entropic driving force for the subsequent release of BtuF required to complete the transport cycle.
Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding.,Karpowich NK, Huang HH, Smith PC, Hunt JF J Biol Chem. 2003 Mar 7;278(10):8429-34. Epub 2002 Dec 4. PMID:12468528<ref>PMID:12468528</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n4a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hunt, J F]]
[[Category: Hunt JF]]
[[Category: Karpowich, N K]]
[[Category: Karpowich NK]]
[[Category: Structural genomic]]
[[Category: Smith PC]]
[[Category: Smith, P C]]
[[Category: Abc transporter]]
[[Category: Nesg]]
[[Category: Periplasmic binding protein]]
[[Category: PSI, Protein structure initiative]]
[[Category: Transmembrane transport]]
[[Category: Transport protein]]
[[Category: Vitamin b12]]

Revision as of 11:45, 10 April 2024

The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12

Structural highlights

1n4a is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

BTUF_ECOLI Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.[1]

Evolutionary Conservation

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

References

  1. ↑ Cadieux N, Bradbeer C, Reeger-Schneider E, Koster W, Mohanty AK, Wiener MC, Kadner RJ. Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli. J Bacteriol. 2002 Feb;184(3):706-17. PMID:11790740

1n4a, resolution 2.00Å

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