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1hlm
From Proteopedia
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AMINO ACID SEQUENCE OF A GLOBIN FROM THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA
Overview
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.
About this Structure
1HLM is a Single protein structure of sequence from Thermomicrobium roseum with , and as ligands. Full crystallographic information is available from OCA.
Reference
Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola., Mauri F, Omnaas J, Davidson L, Whitfill C, Kitto GB, Biochim Biophys Acta. 1991 May 30;1078(1):63-7. PMID:2049384
Page seeded by OCA on Fri Feb 15 15:57:02 2008
