1sra

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==Overview==
==Overview==
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The EF-hand is a highly conserved Ca(2+)-binding motif found in many, cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure, at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair., The two EF-hands interact canonically but their detailed structures are, unusual. In the first EF-hand a one-residue insertion is accommodated by a, cis-peptide bond and by substituting a carboxylate by a peptide carbonyl, as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond., The EF-hand pair interacts tightly with an amphiphilic amino-terminal, helix, reminiscent of target peptide binding by calmodulin. The present, structure defines a novel protein module occurring in several other, extracellular proteins.
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The EF-hand is a highly conserved Ca(2+)-binding motif found in many cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair. The two EF-hands interact canonically but their detailed structures are unusual. In the first EF-hand a one-residue insertion is accommodated by a cis-peptide bond and by substituting a carboxylate by a peptide carbonyl as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond. The EF-hand pair interacts tightly with an amphiphilic amino-terminal helix, reminiscent of target peptide binding by calmodulin. The present structure defines a novel protein module occurring in several other extracellular proteins.
==About this Structure==
==About this Structure==
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[[Category: Hohenadl, C.]]
[[Category: Hohenadl, C.]]
[[Category: Hohenester, E.]]
[[Category: Hohenester, E.]]
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[[Category: Jansonius, J.N.]]
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[[Category: Jansonius, J N.]]
[[Category: Maurer, P.]]
[[Category: Maurer, P.]]
[[Category: Timpl, R.]]
[[Category: Timpl, R.]]
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[[Category: extracellular matrix protein]]
[[Category: extracellular matrix protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:54:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:25 2008''

Revision as of 13:04, 21 February 2008


1sra, resolution 2.0Å

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STRUCTURE OF A NOVEL EXTRACELLULAR CA2+-BINDING MODULE IN BM-40(SLASH)SPARC(SLASH)OSTEONECTIN

Overview

The EF-hand is a highly conserved Ca(2+)-binding motif found in many cytosolic Ca(2+)-modulated proteins. Here we report the crystal structure at 2.0 A resolution of the carboxy-terminal domain of human BM-40 (SPARC, osteonectin), an extracellular matrix protein containing an EF-hand pair. The two EF-hands interact canonically but their detailed structures are unusual. In the first EF-hand a one-residue insertion is accommodated by a cis-peptide bond and by substituting a carboxylate by a peptide carbonyl as a Ca2+ ligand. The second EF-hand is stabilized by a disulphide bond. The EF-hand pair interacts tightly with an amphiphilic amino-terminal helix, reminiscent of target peptide binding by calmodulin. The present structure defines a novel protein module occurring in several other extracellular proteins.

About this Structure

1SRA is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a novel extracellular Ca(2+)-binding module in BM-40., Hohenester E, Maurer P, Hohenadl C, Timpl R, Jansonius JN, Engel J, Nat Struct Biol. 1996 Jan;3(1):67-73. PMID:8548457

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