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4al3
From Proteopedia
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| - | [[Image:4al3.png|left|200px]] | ||
| - | + | ==peptide deformylase (Co-form) with mercaptoethanol== | |
| - | + | <StructureSection load='4al3' size='340' side='right'caption='[[4al3]], [[Resolution|resolution]] 1.98Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4al3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AL3 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]] 1.98Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=4al3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4al3 OCA], [https://pdbe.org/4al3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4al3 RCSB], [https://www.ebi.ac.uk/pdbsum/4al3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4al3 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DEF_ECOLI DEF_ECOLI] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.[HAMAP-Rule:MF_00163] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fluorescently labeled cobalt peptide deformylase (Co-PDF) can be efficiently used as a fluorescence-resonance-energy-transfer-based sensing device for hydrogen sulfide (H(2)S). The proof of concept of our sensor system is substantiated by spectroscopic, structural, and theoretical results. Monohydrogen sulfide coordination to Co-PDF and Ni-PDF was verified by X-ray crystallography. Density functional theory calculations were performed to gain insight into the characteristics of the coordination adduct between H(2)S and the cobalt cofactor in Co-PDF. | ||
| - | + | A FRET Enzyme-Based Probe for Monitoring Hydrogen Sulfide.,Strianese M, Palm GJ, Milione S, Kuhl O, Hinrichs W, Pellecchia C Inorg Chem. 2012 Nov 5;51(21):11220-2. doi: 10.1021/ic301363d. Epub 2012 Oct 16. PMID:23072298<ref>PMID:23072298</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4al3" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Hinrichs | + | __TOC__ |
| - | [[Category: Palm | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Hinrichs W]] | |
| + | [[Category: Palm GJ]] | ||
Current revision
peptide deformylase (Co-form) with mercaptoethanol
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