1mko
From Proteopedia
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'''A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution''' | '''A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution''' | ||
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[[Category: Abraham, D J.]] | [[Category: Abraham, D J.]] | ||
[[Category: Safo, M K.]] | [[Category: Safo, M K.]] | ||
| - | [[Category: | + | [[Category: Allosteric]] |
| - | [[Category: | + | [[Category: Carbonmonoxy-intermediate]] |
| - | [[Category: | + | [[Category: Hemoglobin]] |
| - | [[Category: | + | [[Category: Relaxed state]] |
| - | [[Category: | + | [[Category: Rr2 state]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:19:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:19, 2 May 2008
A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution
Overview
The liganded hemoglobin (Hb) high-salt crystallization condition described by Max Perutz has generated three different crystals of human adult carbonmonoxy hemoglobin (COHbA). The first crystal is isomorphous with the "classical" liganded or R Hb structure. The second crystal reveals a new liganded Hb quaternary structure, RR2, that assumes an intermediate conformation between the R form and another liganded Hb quaternary structure, R2, which was discovered more than a decade ago. Like the R2 structure, the diagnostic R state hydrogen bond between beta2His97 and alpha1Thr38 is missing in the RR2 structure. The third crystal adopts a novel liganded Hb conformation, which we have termed R3, and it shows substantial quaternary structural differences from the R, RR2, and R2 structures. The quaternary structure differences between T and R3 are as large as those between T and R2; however, the T --> R3 and T --> R2 transitions are in different directions as defined by rigid-body screw rotation. Moreover, R3 represents an end state. Compared to all known liganded Hb structures, R3 shows remarkably reduced strain at the alpha-heme, reduced steric contact between the beta-heme ligand and the distal residues, smaller alpha- and beta-clefts, and reduced alpha1-alpha2 and beta1-beta2 iron-iron distances. Together, these unique structural features in R3 should make it the most relaxed and/or greatly enhance its affinity for oxygen compared to the other liganded Hbs. The current Hb structure-function relationships that are now based on T --> R, T -->R --> R2, or T --> R2 --> R transitions may have to be reexamined to take into account the RR2 and R3 liganded structures.
About this Structure
1MKO is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin., Safo MK, Abraham DJ, Biochemistry. 2005 Jun 14;44(23):8347-59. PMID:15938624 Page seeded by OCA on Sat May 3 01:19:07 2008
