1BZ0

HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)

1BZ0 の概要

• エントリーDOI: 10.2210/pdb1bz0/pdb
• 分子名称: PROTEIN (HEMOGLOBIN ALPHA CHAIN), PROTEIN (HEMOGLOBIN BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: oxygen transport, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64547.05

構造登録者

Kavanaugh, J.S.,Arnone, A. (登録日: 1998-11-04, 公開日: 1998-11-11, 最終更新日: 2023-08-09)

主引用文献

Kavanaugh, J.S.,Moo-Penn, W.F.,Arnone, A.
Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge.
Biochemistry, 32:2509-2513, 1993

PubMed Abstract: Hemoglobin Catonsville is a mutation of human hemoglobin (an alpha 2 beta 2 tetramer) in which a glutamate residue is inserted into the first turn of a highly conserved 3(10) helix (the C helix) of each alpha subunit. In theory, amino acid insertions (or deletions) in protein helices can be accommodated via two distinct mechanisms. One, termed the register shift mechanism, preserves the geometry of the helix while requiring all of the residues on one flank of the insertion site to rotate by 100 degrees in the case of an alpha helix or by 120 degrees in the case of a 3(10) helix. The other, termed the bulge (or indentation) mechanism, distorts the local geometry of the helix but does not alter the helix register. High-resolution X-ray diffraction analysis of deoxyhemoglobin Catonsville shows that the inserted residue is accommodated as a bulge, demonstrating that this is a viable mechanism. (In contrast, no such evidence is yet available for the register shift mechanism.) More specifically, the insertion converts one turn of the C helix from 3(10) geometry to alpha helix-like geometry, raising the possibility that a common mechanism for accommodating insertions and deletions within helices may involve localized interconversions between 3(10), alpha, and pi helical structures.

PubMed: 8448109
DOI: 10.1021/bi00061a007

実験手法

X-RAY DIFFRACTION (1.5 Å)