PDBsum entry 1y8h

Oxygen storage/transport

PDB id

1y8h

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Contents

			Protein chains

					141 a.a. *


					146 a.a. *

			Ligands

					HEM ×4

			Waters ×136

* Residue conservation analysis

PDB id:

1y8h

Links

Name:

Oxygen storage/transport

Title:

Horse methemoglobin low salt, ph 7.0

Structure:

Hemoglobin alpha chains. Chain: a, c. Synonym: slow and fast. Other_details: ph 7.0 aquomet structure. Hemoglobin beta chain. Chain: b, d

Source:

Equus caballus. Horse. Organism_taxid: 9796. Organism_taxid: 9796

Biol. unit:

Tetramer (from PQS)

Resolution:

3.10Å

R-factor:

0.202

R-free:

0.274

Authors:

R.Sankaranarayanan,B.K.Biswal,M.Vijayan

Key ref:

R.Sankaranarayanan et al. (2005). A new relaxed state in horse methemoglobin characterized by crystallographic studies. Proteins, 60, 547-551. PubMed id: 15887226 DOI: 10.1002/prot.20510

Date:

13-Dec-04

Release date:

26-Jul-05

PROCHECK

	Headers

	References

Protein chains

P01958 (HBA_HORSE) - Hemoglobin subunit alpha from Equus caballus

Seq: Struc:					142 a.a. 141 a.a.*

Protein chains

P02062 (HBB_HORSE) - Hemoglobin subunit beta from Equus caballus

Seq: Struc:					146 a.a. 146 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1002/prot.20510	Proteins 60:547-551 (2005)
PubMed id: 15887226

A new relaxed state in horse methemoglobin characterized by crystallographic studies.
R.Sankaranarayanan, B.K.Biswal, M.Vijayan.

ABSTRACT

A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states.

Selected figure(s)



	Figure 1. Figure 1. Schematic diagram showing the orientation of 2 2 relative to 1 1 in the r.h.88% structure reported here and other selected relevant structures. The 1 1 dimer in all the structures are superposed (black). The 2 2 dimer and the molecular dyad are shown in different colors: r.h.88%, blue; human R2, magenta; horse deoxy, red; horse met R, green. [1] and [2] values of all the relevant structures with respect to the r.h.88% structure, are given in Table III. Please see text for details.		Figure 2. Figure 2. Switch region in selected relevant structures. The appropriate distances in all the relevant structures are given in Table IV.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17932936

L.Vijayalakshmi, R.Krishna, R.Sankaranarayanan, and M.Vijayan (2008).
An asymmetric dimer of beta-lactoglobulin in a low humidity crystal form--structural changes that accompany partial dehydration and protein action.

Proteins, 71, 241-249.

PDB codes:

2q2m 2q2p 2q39

18540052

P.S.Kaushal, R.Sankaranarayanan, and M.Vijayan (2008).
Water-mediated variability in the structure of relaxed-state haemoglobin.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 463-469.

PDB codes:

2zlt 2zlu 2zlv 2zlw 2zlx

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.