1K1K

Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.

Summary for 1K1K

• Entry DOI: 10.2210/pdb1k1k/pdb
• Related: 1HHO 1RVW
• Descriptor: HEMOGLOBIN ALPHA CHAIN, HEMOGLOBIN BETA CHAIN, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: mutant human hemoglobin c(betae6k), oxygen storage-transport complex, oxygen storage/transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 32329.61

Authors

Dewan, J.C.,Taylor-Feeling, A.,Puius, Y.A.,Patskovska, L.,Patskovsky, Y.,Nagel, R.L.,Almo, S.C.,Hirsch, R.E. (deposition date: 2001-09-25, release date: 2002-12-04, Last modification date: 2023-08-16)

Primary citation

Dewan, J.C.,Feeling-Taylor, A.,Puius, Y.A.,Patskovska, L.,Patskovsky, Y.,Nagel, R.L.,Almo, S.C.,Hirsch, R.E.
Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 58:2038-2042, 2002

PubMed Abstract: Previous studies have demonstrated that in vitro crystallization of R-state liganded hemoglobin C (HbC), a naturally occurring mutant human hemoglobin (betaE6K), in high-phosphate buffer solutions provides a potential model system for the intracellular crystallization of HbC associated with chronic hemolytic anemia in CC disease. The first high-resolution crystal structure of liganded HbC is reported here. HbC was crystallized from high phosphate and the structure of the carbonmonoxy-liganded R-state form was refined at 2.0 A resolution. Crystals exhibit diffraction consistent with the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = 54.16, c = 195.30 A. The structure was solved by difference Fourier techniques and refinement by simulated annealing and restrained least-squares yielded a final R of 0.183 and an R(free) of 0.238 for all 19,382 unique reflections. The side chain of betaK6 exhibits very weak electron density consistent with significant mobility within the crystalline lattice. The highly dynamic nature of the side chain could potentially support a number of specific polar interactions that might reduce the barrier to crystallization and thus result in enhanced crystallization kinetics for HbC relative to HbA. Specifically, the NZ atom of the BK6 side chain could participate in an amino-aromatic hydrogen bond with the pi-electron cloud of betaH116 in a symmetry-related tetramer. BetaK6 NZ might also interact with the main-chain carbonyl O atom of betaH117 and the carboxylate group of betaE22 from a symmetry-related tetramer.

PubMed: 12454462
DOI: 10.1107/S0907444902016426

Experimental method

X-RAY DIFFRACTION (2 Å)