PDBsum entry 1hlm

Oxygen transport

PDB id

1hlm

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Contents

			Protein chain

					159 a.a. *

			Ligands

					CYN-HEM

			Waters ×5

* Residue conservation analysis

PDB id:

1hlm

Links

Name:

Oxygen transport

Title:

Amino acid sequence of a globin from the sea cucumber caudina (molpadia) arenicola

Structure:

Hemoglobin (cyano met). Chain: a. Engineered: yes

Source:

Caudina arenicola. Organism_taxid: 7698

Biol. unit:

Dimer (from PQS)

Resolution:

2.90Å

R-factor:

0.190

Authors:

M.L.Hackert,D.T.Mitchell,S.R.Ernst

Key ref:

F.Mauri et al. (1991). Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola. Biochim Biophys Acta, 1078, 63-67. PubMed id: 2049384 DOI: 10.1016/0167-4838(91)90093-F

Date:

26-Aug-94

Release date:

07-Feb-95

PROCHECK

	Headers

	References

Protein chain

P80017 (GLBD_MOLAR) - Globin D, coelomic from Molpadia arenicola

Seq: Struc:					159 a.a. 158 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1016/0167-4838(91)90093-F	Biochim Biophys Acta 1078:63-67 (1991)
PubMed id: 2049384

Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola.
F.Mauri, J.Omnaas, L.Davidson, C.Whitfill, G.B.Kitto.

ABSTRACT

Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major globins, A, B, C and D. The hemoglobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate globins. The C. arenicola D globin has an equal sequence identity (28%) with both alpha and beta human globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan globins. The C. arenicola D globin shows a 59% identity with the globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17629909

P.Ferragina, R.Giancarlo, V.Greco, G.Manzini, and G.Valiente (2007).
Compression-based classification of biological sequences and structures via the Universal Similarity Metric: experimental assessment.

BMC Bioinformatics, 8, 252.

9723169

G.B.Kitto, P.W.Thomas, and M.L.Hackert (1998).
Evolution of cooperativity in hemoglobins: what can invertebrate hemoglobins tell us?

J Exp Zool, 282, 120-126.

8940909

F.Shishikura (1996).
Amino acid sequence of the monomer subunit of the extracellular hemoglobin of the earthworm, Pheretima hilgendorfi.

Zoolog Sci, 13, 551-558.

1515032

G.D.McDonald, L.Davidson, and G.B.Kitto (1992).
Amino acid sequence of the coelomic C globin from the sea cucumber Caudina (Molpadia) arenicola.

J Protein Chem, 11, 29-37.

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.