1JNI

Structure of the NapB subunit of the periplasmic nitrate reductase from Haemophilus influenzae.

Summary for 1JNI

• Entry DOI: 10.2210/pdb1jni/pdb
• Descriptor: DIHEME CYTOCHROME C NAPB, HEME C (3 entities in total)
• Functional Keywords: dihaem cytochrome c, proteolytic fragment, nitrate reductase subunit, oxidoreductase
• Biological source: Haemophilus influenzae
• Cellular location: Periplasm (By similarity): P44654
• Total number of polymer chains: 1
• Total formula weight: 14681.04

Authors

Brige, A.,Leys, D.,Meyer, T.E.,Cusanovich, M.A.,Van Beeumen, J.J. (deposition date: 2001-07-24, release date: 2002-05-17, Last modification date: 2024-11-06)

Primary citation

Brige, A.,Leys, D.,Meyer, T.E.,Cusanovich, M.A.,Van Beeumen, J.J.
The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement.
Biochemistry, 41:4827-4836, 2002

PubMed Abstract: The diheme cytochrome NapB constitutes the small subunit of a periplasmic nitrate reductase found in a wide variety of bacterial species, including pathogens. The NapB protein is essential in transferring electrons to the large catalytic subunit NapA, which subsequently reduces nitrate to nitrite. Here we present the crystal structure of a proteolyzed form of recombinant NapB from Haemophilus influenzae, which was determined by the multiple-wavelength anomalous dispersion (MAD) method at 1.25 A resolution. This structure shows an unprecedented fold, confirming that NapB proteins belong to a new class of cytochromes. The two heme groups have nearly parallel heme planes and are stacked at van der Waals distances with an iron-to-iron distance of only 9.9 A, two structural features that are also present in the split-Soret diheme cytochrome c from Desulfovibrio desulfuricans ATCC 27774, which is otherwise unrelated in the peptide chain folding pattern. The two propionate side chains on both heme groups are hydrogen-bonded to each other, a structural characteristic that to date also has not been reported in any other heme protein. The propionates of one of the heme groups are pulled toward the interior of the molecule due to a salt bridge and a number of hydrogen bonds between the propionates and conserved residues. We propose a hypothetical but plausible model of the NapAB complex in which the four redox centers are positioned in a virtually linear configuration which spans a distance of nearly 40 A, suggesting an efficient pathway for the transfer of electrons from NapC, the physiological electron donor of NapB, to a nitrate molecule at the catalytic site of NapA.

PubMed: 11939777
DOI: 10.1021/bi012144b

Experimental method

X-RAY DIFFRACTION (1.25 Å)