4ave

C.lacteus nerve Hb in the deoxy form

spinqualitylabelsall models 4ave, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ave is a 1 chain structure with sequence from Cerla. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, GOL, HEM, SO4 Related: 1kr7, 1v07, 2vyy, 2vyz, 2xkg, 2xkh, 2xki, 4avd Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLBN_CERLA] Acts as an oxygen store capable of sustaining neuronal activity in an anoxic environment for 5 to 30 min. Publication Abstract from PubMed The nerve tissue mini-hemoglobin from Cerebratulus lacteus (CerHb) displays an essential globin fold hosting a protein matrix tunnel held to allow traffic of small ligands to and from the heme. CerHb heme pocket hosts the distal TyrB10/GlnE7 pair, normally linked to low rates of O(2) dissociation and ultra-high O(2) affinity. However, CerHb affinity for O(2) is similar to that of mammalian myoglobins, due to a dynamic equilibrium between high and low affinity states driven by the ability of ThrE11 to orient the TyrB10 OH group relative to the heme ligand. We present here the high resolution crystal structures of CerHb in the unligated and carbomonoxy states. Although CO binds to the heme with an orientation different from the O(2) ligand, the overall binding schemes for CO and O(2) are essentially the same, both ligands being stabilized through a network of hydrogen bonds based on TyrB10, GlnE7, and ThrE11. No dramatic protein structural changes are needed to support binding of the ligands, which can freely reach the heme distal site through the apolar tunnel. A lack of main conformational changes between the heme-unligated and -ligated states grants stability to the folded mini-Hb and is a prerequisite for fast ligand diffusion to/from the heme. High Resolution Crystal Structures of the Cerebratulus lacteus Mini-Hb in the Unligated and Carbomonoxy States.,Germani F, Pesce A, Venturini A, Moens L, Bolognesi M, Dewilde S, Nardini M Int J Mol Sci. 2012;13(7):8025-37. doi: 10.3390/ijms13078025. Epub 2012 Jun 28. PMID:22942687 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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