1hlu

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[[Image:1hlu.gif|left|200px]]<br />
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[[Image:1hlu.gif|left|200px]]<br /><applet load="1hlu" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1hlu" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hlu, resolution 2.65&Aring;" />
caption="1hlu, resolution 2.65&Aring;" />
'''STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE'''<br />
'''STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE'''<br />
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==About this Structure==
==About this Structure==
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1HLU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA, ACE and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1HLU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb19_1.html Actin]]. Structure known Active Sites: CAT and NUC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLU OCA].
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1HLU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA, ACE and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1HLU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb19_1.html Actin]]. Known structural/functional Sites: <scene name='pdbsite=CAT:Ca (Divalent Cation) Binding Site w. Atp. Unlike Pdb Ent ...'>CAT</scene> and <scene name='pdbsite=NUC:Atp Binding Site, Taken From Pdb Entry 2btf'>NUC</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLU OCA].
==Reference==
==Reference==
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[[Category: profilin]]
[[Category: profilin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:38:41 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:32:25 2007''

Revision as of 14:22, 18 December 2007


1hlu, resolution 2.65Å

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STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE

Overview

The structure of an "open state" of crystalline profilin:beta-actin has, been solved to 2.65 A by X-ray crystallography. The open-state crystals, in 1.8 M potassium phosphate, have an expanded unit cell dimension in the, c direction of 185.7 A compared with 171.9 A in the previously solved, ammonium sulphate-stabilized "tight-state" structure. The unit cell change, between the open and the tight states is accompanied by large subdomain, movements in actin. Furthermore, the nucleotide in the open state is, significantly more exposed to solvent, and local conformational changes in, the hydrophobic pocket surrounding cysteine 374 occur during the, transition to the tight state. Significant changes were observed at the N, terminus and in the DNase-I binding loop. Neither the structure of, profilin nor its contact with beta-actin are affected by the changes in, the unit cell. Applying osmotic pressure to profilin:beta-actin crystals, brings about a collapse of the unit cell comparable with that seen in the, open to tight-state transition, enabling an estimate of the work required, to cause this transformation of beta-actin in the crystals. The slight, difference in energy between the open and collapsed states explains the, extreme sensitivity of profilin:beta-actin crystals to changes in chemical, and thermal environment.

About this Structure

1HLU is a Protein complex structure of sequences from Bos taurus with CA, ACE and ATP as ligands. The following page contains interesting information on the relation of 1HLU with [Actin]. Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

The structure of an open state of beta-actin at 2.65 A resolution., Chik JK, Lindberg U, Schutt CE, J Mol Biol. 1996 Nov 8;263(4):607-23. PMID:8918942

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