3m0b

Ru-Porphyrin Protein Scaffolds for Sensing O2Ru-Porphyrin Protein Scaffolds for Sensing O2

Structural highlights 3m0b is a 1 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RBX6_CALS4 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 PubMed Hemoprotein-based scaffolds containing phosphorescent ruthenium(II) CO mesoporphyrin IX (RuMP) are reported here for oxygen (O(2)) sensing in biological contexts. RuMP was incorporated into the protein scaffolds during protein expression utilizing a novel method that we have described previously. A high-resolution (2.00 A) crystal structure revealed that the unnatural porphyrin binds to the proteins in a manner similar to the native heme and does not perturb the protein fold. The protein scaffolds were found to provide unique coordination environments for RuMP and modulate the porphyrin emission properties. Emission lifetime measurements demonstrate a linear O(2) response within the physiological range and precision comparable to commercial O(2) sensors. The RuMP proteins are robust, readily modifiable platforms and display promising O(2) sensing properties for future in vivo applications. Ru-porphyrin protein scaffolds for sensing O2.,Winter MB, McLaurin EJ, Reece SY, Olea C Jr, Nocera DG, Marletta MA J Am Chem Soc. 2010 Apr 28;132(16):5582-3. PMID:20373741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures Methyl-accepting chemotaxis protein

spinqualitylabelsall models 3m0b, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image