1hlm

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermomicrobium roseum]]
[[Category: Thermomicrobium roseum]]
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[[Category: Ernst, S.R.]]
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[[Category: Ernst, S R.]]
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[[Category: Hackert, M.L.]]
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[[Category: Hackert, M L.]]
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[[Category: Mitchell, D.T.]]
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[[Category: Mitchell, D T.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CYN]]
[[Category: CYN]]
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[[Category: oxygen transport]]
[[Category: oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:30 2008''

Revision as of 11:02, 21 February 2008


1hlm, resolution 2.9Å

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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

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