7vcm: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7vcm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VCM FirstGlance]. <br> | <table><tr><td colspan='2'>[[7vcm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VCM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.85Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=7vcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vcm OCA], [https://pdbe.org/7vcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vcm RCSB], [https://www.ebi.ac.uk/pdbsum/7vcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vcm ProSAT]</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=7vcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vcm OCA], [https://pdbe.org/7vcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vcm RCSB], [https://www.ebi.ac.uk/pdbsum/7vcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vcm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/KBP_ECOLI KBP_ECOLI] Highly specific potassium binding protein that is required for normal growth in the presence of high levels of external K(+). May act as a sensor of cytoplasmic K(+) concentration. Binds a single K(+) ion, which induces a large conformational change. Can also bind the larger alkali metal ions Rb(+) and Cs(+), and NH(4)(+) (PubMed:27112601). May be involved in the regulation of peptidoglycan cross-linking (PubMed:25422305).<ref>PMID:25422305</ref> <ref>PMID:27112601</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | [https://www.uniprot.org/uniprot/KBP_ECOLI KBP_ECOLI] Highly specific potassium binding protein that is required for normal growth in the presence of high levels of external K(+). May act as a sensor of cytoplasmic K(+) concentration. Binds a single K(+) ion, which induces a large conformational change. Can also bind the larger alkali metal ions Rb(+) and Cs(+), and NH(4)(+) (PubMed:27112601). May be involved in the regulation of peptidoglycan cross-linking (PubMed:25422305).<ref>PMID:25422305</ref> <ref>PMID:27112601</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | ||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:23, 29 November 2023
crystal structure of GINKO1crystal structure of GINKO1
Structural highlights
FunctionKBP_ECOLI Highly specific potassium binding protein that is required for normal growth in the presence of high levels of external K(+). May act as a sensor of cytoplasmic K(+) concentration. Binds a single K(+) ion, which induces a large conformational change. Can also bind the larger alkali metal ions Rb(+) and Cs(+), and NH(4)(+) (PubMed:27112601). May be involved in the regulation of peptidoglycan cross-linking (PubMed:25422305).[1] [2] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. See AlsoReferences
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