1b5s

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[[Image:1b5s.jpg|left|200px]]
[[Image:1b5s.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1b5s |SIZE=350|CAPTION= <scene name='initialview01'>1b5s</scene>, resolution 4.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1b5s", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1b5s| PDB=1b5s | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5s OCA], [http://www.ebi.ac.uk/pdbsum/1b5s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5s RCSB]</span>
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'''DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS'''
'''DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS'''
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[[Category: Perham, R N.]]
[[Category: Perham, R N.]]
[[Category: Westphal, A H.]]
[[Category: Westphal, A H.]]
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[[Category: dihydrolipoyl acetyltransferase]]
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[[Category: Dihydrolipoyl acetyltransferase]]
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[[Category: dihydrolipoyl transacetylase]]
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[[Category: Dihydrolipoyl transacetylase]]
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[[Category: e2p]]
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[[Category: E2p]]
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[[Category: pyruvate dehydrogenase]]
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[[Category: Pyruvate dehydrogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:06:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:14 2008''
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Revision as of 08:06, 2 May 2008

Image:1b5s.jpg

Template:STRUCTURE 1b5s

DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS


Overview

The pyruvate dehydrogenase multienzyme complex (Mr of 5-10 million) is assembled around a structural core formed of multiple copies of dihydrolipoyl acetyltransferase (E2p), which exhibits the shape of either a cube or a dodecahedron, depending on the source. The crystal structures of the 60-meric dihydrolipoyl acyltransferase cores of Bacillus stearothermophilus and Enterococcus faecalis pyruvate dehydrogenase complexes were determined and revealed a remarkably hollow dodecahedron with an outer diameter of approximately 237 A, 12 large openings of approximately 52 A diameter across the fivefold axes, and an inner cavity with a diameter of approximately 118 A. Comparison of cubic and dodecahedral E2p assemblies shows that combining the principles of quasi-equivalence formulated by Caspar and Klug [Caspar, D. L. & Klug, A. (1962) Cold Spring Harbor Symp. Quant. Biol. 27, 1-4] with strict Euclidean geometric considerations results in predictions of the major features of the E2p dodecahedron matching the observed features almost exactly.

About this Structure

1B5S is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes., Izard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG, Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1240-5. PMID:9990008 Page seeded by OCA on Fri May 2 11:06:19 2008

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