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< | ==PHOSPHATE-BINDING PROTEIN MUTANT A197C== | ||
<StructureSection load='1a55' size='340' side='right'caption='[[1a55]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a55]] is a 1 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=1A55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A55 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]] 2.4Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</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=1a55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a55 OCA], [https://pdbe.org/1a55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a55 RCSB], [https://www.ebi.ac.uk/pdbsum/1a55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a55 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import. | |||
== 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/a5/1a55_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=1a55 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystal structures are presented for the A197C mutant of Escherichia coli phosphate binding protein (PBP) and the same mutant labeled at Cys197 with N-[2-(1-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC). Both proteins are complexed with inorganic phosphate. The latter molecule, MDCC-PBP, exhibits a large increase in fluorescence on binding inorganic phosphate. The resulting high-fluorescence state of the coumarin and the ability of this coumarin to monitor the conformational changes associated with inorganic phosphate binding are interpreted in terms of the specific interactions of MDCC with the protein. The structure helps to explain why this particular label gives a high-fluorescence state on binding inorganic phosphate, while several other related labels do not, and hence aids our general understanding of environmentally sensitive fluorescence probes on proteins. | |||
Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.,Hirshberg M, Henrick K, Haire LL, Vasisht N, Brune M, Corrie JE, Webb MR Biochemistry. 1998 Jul 21;37(29):10381-5. PMID:9671506<ref>PMID:9671506</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1a55" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphate-binding protein|Phosphate-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Brune | [[Category: Brune M]] | ||
[[Category: Corrie | [[Category: Corrie JET]] | ||
[[Category: Henrick | [[Category: Henrick K]] | ||
[[Category: Hirshberg | [[Category: Hirshberg M]] | ||
[[Category: Lloyd-Haire | [[Category: Lloyd-Haire L]] | ||
[[Category: Vasisht | [[Category: Vasisht N]] | ||
[[Category: Webb | [[Category: Webb MR]] | ||
Latest revision as of 13:47, 2 August 2023
PHOSPHATE-BINDING PROTEIN MUTANT A197CPHOSPHATE-BINDING PROTEIN MUTANT A197C
Structural highlights
FunctionPSTS_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 PubMedCrystal structures are presented for the A197C mutant of Escherichia coli phosphate binding protein (PBP) and the same mutant labeled at Cys197 with N-[2-(1-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC). Both proteins are complexed with inorganic phosphate. The latter molecule, MDCC-PBP, exhibits a large increase in fluorescence on binding inorganic phosphate. The resulting high-fluorescence state of the coumarin and the ability of this coumarin to monitor the conformational changes associated with inorganic phosphate binding are interpreted in terms of the specific interactions of MDCC with the protein. The structure helps to explain why this particular label gives a high-fluorescence state on binding inorganic phosphate, while several other related labels do not, and hence aids our general understanding of environmentally sensitive fluorescence probes on proteins. Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.,Hirshberg M, Henrick K, Haire LL, Vasisht N, Brune M, Corrie JE, Webb MR Biochemistry. 1998 Jul 21;37(29):10381-5. PMID:9671506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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