Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.

@article{citeulike:2783973, abstract = {The central tunnel of the eight-bladed beta-propeller domain of cytochrome cd1 (nitrite reductase) is seen, from a 1.28 A resolution structure, to contain hydrogen donors and acceptors that are satisfied by interaction either with water or the d1 haem. The d1 haem, although bound by an extensive network of hydrogen bonds, is not distorted in its binding pocket and is confirmed to have exactly the dioxoisobacteriochlorin structure proposed from chemical studies. A biological rationale is advanced for the undistorted structure of the d1 haem and the large number of hydrogen bonds it makes. The beta-propeller domain can be closely superimposed on that of methanol dehydrogenase despite the enzymes sharing no common sequence motifs and using a different set of interactions to "Velcro" close the propeller. The sequence and likely structural relationships between cytochrome cd1 or methanol dehydrogenase and other predicted eight-bladed beta-propeller domains in proteins, such as the pyrolloquinoline quinone-dependent alcohol dehydrogenase, are discussed and compared with other propeller proteins. From sequencing the nirS gene of Thiosphaera pantotropha, it is established that the amino acid sequence deduced previously in part from X-ray diffraction data at lower resolution was largely correct, as was the proposal that eight N-terminal amino acid residues were not seen in the structure. The unusual haem iron environments in both the c-type cytochrome domain, with His/His coordination, and the d1-type cytochrome domain with Tyr/His coordination are related to the functions of the redox centres.}, address = {Department of Biochemistry, University of Oxford, UK.}, author = {Baker, S. C. and Saunders, N. F. and Willis, A. C. and Ferguson, S. J. and Hajdu, J. and F\"{u}l\"{o}p, V. }, citeulike-article-id = {2783973}, doi = {10.1006/jmbi.1997.1070}, issn = {0022-2836}, journal = {Journal of molecular biology}, keywords = {beta-propeller, cytochrome, haem, nitrite, protein, reductase, structure}, month = {June}, number = {3}, pages = {440--455}, posted-at = {2008-05-11 10:19:58}, priority = {2}, title = {Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.}, url = {http://dx.doi.org/10.1006/jmbi.1997.1070}, volume = {269}, year = {1997} }

TY - JOUR ID - citeulike:2783973 TI - Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds. JF - Journal of molecular biology VL - 269 IS - 3 SP - 440 EP - 455 AD - Department of Biochemistry, University of Oxford, UK. SN - 0022-2836 N2 - The central tunnel of the eight-bladed beta-propeller domain of cytochrome cd1 (nitrite reductase) is seen, from a 1.28 A resolution structure, to contain hydrogen donors and acceptors that are satisfied by interaction either with water or the d1 haem. The d1 haem, although bound by an extensive network of hydrogen bonds, is not distorted in its binding pocket and is confirmed to have exactly the dioxoisobacteriochlorin structure proposed from chemical studies. A biological rationale is advanced for the undistorted structure of the d1 haem and the large number of hydrogen bonds it makes. The beta-propeller domain can be closely superimposed on that of methanol dehydrogenase despite the enzymes sharing no common sequence motifs and using a different set of interactions to "Velcro" close the propeller. The sequence and likely structural relationships between cytochrome cd1 or methanol dehydrogenase and other predicted eight-bladed beta-propeller domains in proteins, such as the pyrolloquinoline quinone-dependent alcohol dehydrogenase, are discussed and compared with other propeller proteins. From sequencing the nirS gene of Thiosphaera pantotropha, it is established that the amino acid sequence deduced previously in part from X-ray diffraction data at lower resolution was largely correct, as was the proposal that eight N-terminal amino acid residues were not seen in the structure. The unusual haem iron environments in both the c-type cytochrome domain, with His/His coordination, and the d1-type cytochrome domain with Tyr/His coordination are related to the functions of the redox centres. KW - beta-propeller KW - cytochrome KW - haem KW - nitrite KW - protein KW - reductase KW - structure AU - Baker, SC AU - Saunders, NF AU - Willis, AC AU - Ferguson, SJ AU - Hajdu, J AU - Fülöp, V PY - 1997/06/13/ UR - http://dx.doi.org/10.1006/jmbi.1997.1070 ER -