1hlm
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1hlm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlm, resolution 2.9Å" /> '''AMINO ACID SEQUENCE ...)
Next diff →
Revision as of 11:02, 8 November 2007
|
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 CYN, ACE and HEM 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 Thu Nov 8 13:08:22 2007
