1gvh

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File:1gvh.gif


1gvh, resolution 2.19Å

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THE X-RAY STRUCTURE OF FERRIC ESCHERICHIA COLI FLAVOHEMOGLOBIN REVEALS AN UNESPECTED GEOMETRY OF THE DISTAL HEME POCKET

OverviewOverview

The x-ray structure of ferric unliganded lipid-free Escherichia coli, flavohemoglobin has been solved to a resolution of 2.2 A and refined to an, R-factor of 19%. The overall fold is similar to that of ferrous, lipid-bound Alcaligenes eutrophus flavohemoglobin with the notable, exception of the E helix positioning within the globin domain and a, rotation of the NAD binding module with respect to the FAD-binding domain, accompanied by a substantial rearrangement of the C-terminal region. An, inspection of the heme environment in E. coli flavohemoglobin reveals an, unexpected architecture of the distal pocket. In fact, the distal site is, occupied by the isopropyl side chain Leu-E11 that shields the heme iron, from the residues in the topological positions predicted to interact with, heme ... [(full description)]

About this StructureAbout this Structure

1GVH is a [Single protein] structure of sequence from [Escherichia coli] with NA, CL, FAD and HEM as [ligands]. Active as [Transferred entry: 1.5.1.34], with EC number [1.6.99.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket., Ilari A, Bonamore A, Farina A, Johnson KA, Boffi A, J Biol Chem. 2002 Jun 28;277(26):23725-32. Epub 2002 Apr 18. PMID:11964402

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