1ixg: Difference between revisions

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==PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE==
==PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE==
<StructureSection load='1ixg' size='340' side='right' caption='[[1ixg]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
<StructureSection load='1ixg' size='340' side='right' caption='[[1ixg]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHO-S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHO-S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ixg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ixg OCA], [http://pdbe.org/1ixg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ixg RCSB], [http://www.ebi.ac.uk/pdbsum/1ixg PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ixg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ixg OCA], [http://pdbe.org/1ixg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ixg RCSB], [http://www.ebi.ac.uk/pdbsum/1ixg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ixg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=1ixg ConSurf].
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Revision as of 12:42, 4 October 2017

PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATEPHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE

Structural highlights

1ixg is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:PHO-S ("Bacillus coli" Migula 1895)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.

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

A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.,Wang Z, Luecke H, Yao N, Quiocho FA Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942[1]

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

See Also

References

  1. Wang Z, Luecke H, Yao N, Quiocho FA. A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942

1ixg, resolution 1.05Å

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OCA