1bu3
From Proteopedia
(New page: 200px<br /><applet load="1bu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bu3, resolution 1.65Å" /> '''REFINED CRYSTAL STRU...) |
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| - | [[Image:1bu3.jpg|left|200px]]<br /><applet load="1bu3" size=" | + | [[Image:1bu3.jpg|left|200px]]<br /><applet load="1bu3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bu3, resolution 1.65Å" /> | caption="1bu3, resolution 1.65Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF CALCIUM-BOUND SILVER HAKE (PI 4.2) PARVALBUMIN AT 1.65 A.'''<br /> | '''REFINED CRYSTAL STRUCTURE OF CALCIUM-BOUND SILVER HAKE (PI 4.2) PARVALBUMIN AT 1.65 A.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Parvalbumins are a class of calcium-binding proteins characterized by the | + | Parvalbumins are a class of calcium-binding proteins characterized by the presence of several helix-loop-helix (EF-hand) motifs. It is suspected that these proteins evolved via intragene duplication from a single EF-hand. Silver hake parvalbumin (SHPV) consists of three EF-type helix-loop-helix regions, two of which have the ability to bind calcium. The three helix-loop-helix motifs are designated AB, CD, and EF, respectively. In this study, native silver hake parvalbumin isoform B (SHPV-B) has been sequenced by mass spectrometry. The sequence indicates that this parvalbumin is a beta-lineage parvalbumin. SHPV-B was cleaved into two major fragments, consisting of the ABCD and EF regions of the native protein. The 33-amino acid EF fragment (residues 76-108), containing one of the calcium ion binding sites in native SHPV-B, has been isolated and studied for its structural characteristics, ability to bind divalent and trivalent cations, and for its propensity to undergo metal ion-induced self-association. The presence of Ca2+ does not induce significant secondary structure in the EF fragment. However, NMR and CD results indicate significant secondary structure promotion in the EF fragment in the presence of the higher charge-density trivalent cations. Sedimentation equilibrium analysis results show that the EF fragment exists in a monomer-dimer equilibrium when complexed with La3+. |
==About this Structure== | ==About this Structure== | ||
| - | 1BU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Merluccius_bilinearis Merluccius bilinearis] with CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Merluccius_bilinearis Merluccius bilinearis] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Merluccius bilinearis]] | [[Category: Merluccius bilinearis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Harrington, D | + | [[Category: Harrington, D J.]] |
| - | [[Category: Nelson, D | + | [[Category: Nelson, D J.]] |
| - | [[Category: Richardson, R | + | [[Category: Richardson, R C.]] |
| - | [[Category: Royer, W | + | [[Category: Royer, W E.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium binding]] | [[Category: calcium binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:08 2008'' |
Revision as of 09:59, 21 February 2008
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REFINED CRYSTAL STRUCTURE OF CALCIUM-BOUND SILVER HAKE (PI 4.2) PARVALBUMIN AT 1.65 A.
Overview
Parvalbumins are a class of calcium-binding proteins characterized by the presence of several helix-loop-helix (EF-hand) motifs. It is suspected that these proteins evolved via intragene duplication from a single EF-hand. Silver hake parvalbumin (SHPV) consists of three EF-type helix-loop-helix regions, two of which have the ability to bind calcium. The three helix-loop-helix motifs are designated AB, CD, and EF, respectively. In this study, native silver hake parvalbumin isoform B (SHPV-B) has been sequenced by mass spectrometry. The sequence indicates that this parvalbumin is a beta-lineage parvalbumin. SHPV-B was cleaved into two major fragments, consisting of the ABCD and EF regions of the native protein. The 33-amino acid EF fragment (residues 76-108), containing one of the calcium ion binding sites in native SHPV-B, has been isolated and studied for its structural characteristics, ability to bind divalent and trivalent cations, and for its propensity to undergo metal ion-induced self-association. The presence of Ca2+ does not induce significant secondary structure in the EF fragment. However, NMR and CD results indicate significant secondary structure promotion in the EF fragment in the presence of the higher charge-density trivalent cations. Sedimentation equilibrium analysis results show that the EF fragment exists in a monomer-dimer equilibrium when complexed with La3+.
About this Structure
1BU3 is a Single protein structure of sequence from Merluccius bilinearis with and as ligands. Full crystallographic information is available from OCA.
Reference
Characterization of a helix-loop-helix (EF hand) motif of silver hake parvalbumin isoform B., Revett SP, King G, Shabanowitz J, Hunt DF, Hartman KL, Laue TM, Nelson DJ, Protein Sci. 1997 Nov;6(11):2397-408. PMID:9385642
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