PDBsum entry 1jf3

Oxygen storage/transport

PDB id: 1jf3

Contents

Protein chain

147 a.a. *

Ligands

HEM

Waters ×81

* Residue conservation analysis

PDB id:

1jf3

Name:

Oxygen storage/transport

Title:

Crystal structure of component iii glycera dibranchiata monomeric hemoglobin

Structure:

Monomer hemoglobin component iii. Chain: a

Source:

Glycera dibranchiata. Organism_taxid: 6350

Resolution:

1.40Å R-factor: 0.189 R-free: 0.215

Authors:

H.J.Park,C.Yang,N.Treff,J.D.Satterlee,C.H.Kang

Key ref:

H.J.Park et al. (2002). Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV. Proteins, 49, 49-60. PubMed id: 12211015 DOI: 10.1002/prot.10199

Date:

20-Jun-01 Release date: 20-Jun-02

Protein chain

P02216  (GLB1_GLYDI) -  Globin, major monomeric component from Glycera dibranchiata

Seq: 147 a.a.

Struc: 147 a.a.*

* PDB and UniProt seqs differ at 10 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/prot.10199

Proteins 49:49-60 (2002)

PubMed id: 12211015

Crystal structures of unligated and CN-ligated Glycera dibranchiata monomer ferric hemoglobin components III and IV.

H.J.Park, C.Yang, N.Treff, J.D.Satterlee, C.Kang.

ABSTRACT

Erythrocytes of the marine annelid, Glycera dibranchiata, contain a mixture of monomeric and polymeric hemoglobins. There are three major monomer hemoglobin components, II, III, IV (also called GMH2, 3, and 4), that have been highly purified and well characterized. We have now crystallized GMH3 and GMH4 and determined their structures to 1.4-1.8 A resolution. The structures were determined for these two monomer hemoglobins in the oxidized (Fe3+, ferric, or met-) forms in both the unligated and cyanide-ligated states. This work differs from two published, refined structures of a Glycera dibranchiata monomer hemoglobin, which has a sequence that is substantially different from any bona fide major monomer hemoglobins (GMH2, 3, or 4). The high-resolution crystal structures (presented here) and the previous NMR structure of CO-ligated GMH4, provide a basis for interpreting structure/function details of the monomer hemoglobins. These details include: (1) the strong correlation between temperature factor and NMR dynamics for respective protein forms; (2) the unique nature of the HisE7Leu primary sequence substitutions in GMH3 and GMH4 and their impact on cyanide ion binding kinetics; (3) the LeuB10Phe difference between GMH3 and GMH4 and its impact on ligand binding; and (4) elucidation of changes in the structural details of the distal and proximal heme pockets upon cyanide binding.

Selected figure(s)

Figure 4.
Figure 4. Illustration of heme-b, the prosthetic group of the G. dibranchiata monomer hemoglobins, labeled according to the crystallographic convention. Fischer numberings of the pyrrole carbons are shown in parentheses.

Figure 8.
Figure 8. Superimposed views of heme and selected heme pocket amino acid residues of: (A) GMH3: unligated (red) and CN-ligated (green); and (B) GMH4: unligated (blue) and CN-ligated (yellow-green).

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2002, 49, 49-60) copyright 2002.

Figures were selected by an automated process.