1QHE

ENERGETICS OF A HYDROGEN BOND (CHARGED AND NEUTRAL) AND OF A CATION-PI INTERACTION IN APOFLAVODOXIN

Summary for 1QHE

• Entry DOI: 10.2210/pdb1qhe/pdb
• Related: 1FTG
• Descriptor: PROTEIN (FLAVODOXIN), SULFATE ION (3 entities in total)
• Functional Keywords: flavodoxin, electron transport
• Biological source: Nostoc sp.
• Total number of polymer chains: 1
• Total formula weight: 18856.51

Authors

Romero, A.,Fernandez-Recio, J.,Sancho, J. (deposition date: 1999-05-12, release date: 1999-05-20, Last modification date: 2023-08-16)

Primary citation

Fernandez-Recio, J.,Romero, A.,Sancho, J.
Energetics of a hydrogen bond (charged and neutral) and of a cation-pi interaction in apoflavodoxin.
J.Mol.Biol., 290:319-330, 1999

PubMed Abstract: Anabaena apoflavodoxin contains a single histidine residue (H34) that interacts with two aromatic residues (F7 and Y47). The histidine and phenylalanine rings are almost coplanar and they can establish a cation-pi interaction when the histidine is protonated. The histidine and tyrosine side-chains are engaged in a hydrogen bond, which is their only contact. We analyse the energetics of these interactions using p Ka-shift analysis, double-mutant cycle analysis at two pH values, and X-ray crystallography. The H/F interaction is very weak when the histidine is neutral, but it is strengthened by 0.5 kcal mol-1on histidine protonation. Supporting this fact, the histidine p Kain a F7L mutant is 0.4 pH units lower than in wild-type. The strength of the H/Y hydrogen bond is 0.7 kcal mol-1when the histidine is charged, and it becomes stronger (1.3 kcal mol-1) when the histidine is neutral. This is consistent with our observation that the (H34)Nepsilon2-OH(Y47) distance is slightly shorter in the apoflavodoxin structure at pH 9.0 than in the previously reported structure at pH 6.0. It is also consistent with a histidine p Kavalue 0.6 pH units higher in a Y47F mutant than in the wild-type protein. We suggest that the higher stability of the neutral hydrogen bond could be due to a higher desolvation penalty of the charged hydrogen bond that would offset its more favourable enthalpy of formation. The relationship between hydrogen bond strength and the contribution of hydrogen bonds to protein stability is discussed.

PubMed: 10388575
DOI: 10.1006/jmbi.1999.2863

Experimental method

X-RAY DIFFRACTION (2 Å)