1HLM

AMINO ACID SEQUENCE OF A GLOBIN FROM THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA

Summary for 1HLM

• Entry DOI: 10.2210/pdb1hlm/pdb
• Descriptor: HEMOGLOBIN (CYANO MET), CYANIDE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Caudina arenicola
• Total number of polymer chains: 1
• Total formula weight: 18369.84

Authors

Hackert, M.L.,Mitchell, D.T.,Ernst, S.R. (deposition date: 1994-08-26, release date: 1995-02-07, Last modification date: 2024-10-09)

Primary citation

Mauri, F.,Omnaas, J.,Davidson, L.,Whitfill, C.,Kitto, G.B.
Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola.
Biochim.Biophys.Acta, 1078:63-67, 1991

PubMed 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.

PubMed: 2049384
DOI: 10.1016/0167-4838(91)90093-F

Experimental method

X-RAY DIFFRACTION (2.9 Å)