4al3 | pdb_00004al3

peptide deformylase (Co-form) with mercaptoethanol

spinqualitylabelsall models 4al3, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4al3 is a 1 chain structure with sequence from Escherichia coli bl21(de3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME, CL, CO NonStd Res: CSO Related: 1bs4, 1bs5, 1bs6, 1bs7, 1bs8, 1bsj, 1bsk, 1bsz, 1def, 1dff, 1dtf, 1g27, 1g2a, 1icj, 1lru, 1xem, 1xen, 1xeo, 2ai8, 2def, 2dtf, 2vhm, 2w3t, 2w3u, 4al2 Activity: Peptide deformylase, with EC number 3.5.1.88 Resources: FirstGlance, OCA, RCSB, PDBsum Function [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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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