3vol

X-ray Crystal Structure of PAS-HAMP Aer2 in the CN-bound Form

spinqualitylabelsall models 3vol, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vol is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.399Å Ligands: CYN, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCPB_PSEAE Chemoreceptor that plays a critical role in the virulence and pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598). Probably acts through oxygen sensing (PubMed:28167524, PubMed:31511598, PubMed:34383467). Uses a heme-based sensor (PubMed:21255112, PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407, PubMed:14987771). When expressed in E.coli, is able to sense and mediate repellent responses to oxygen, carbon monoxide and nitric oxide (PubMed:21255112). Publication Abstract from PubMed The crystal structure of a truncated Aer2, a signal transducer protein from Pseudomonas aeruginosa, consisting of the heme-containing PAS and di-HAMP domains revealed that a distal tryptophan residue (Trp283) plays an important role in stabilizing the heme-bound O(2) and intra-molecular signal transduction upon O(2) binding. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa.,Sawai H, Sugimoto H, Shiro Y, Ishikawa H, Mizutani Y, Aono S Chem Commun (Camb). 2012 Jul 4;48(52):6523-5. doi: 10.1039/c2cc32549g. Epub 2012 , May 23. PMID:22622145 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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