2fak

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{{STRUCTURE_2fak| PDB=2fak | SCENE= }}
{{STRUCTURE_2fak| PDB=2fak | SCENE= }}
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'''Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome'''
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===Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome===
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==Overview==
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The crystal structures of the yeast 20S proteasome core particle (CP) in complex with Salinosporamides A (NPI-0052; 1) and B (4) were solved at &lt;3 angstroms resolution. Each ligand is covalently bound to Thr1O(gamma) via an ester linkage to the carbonyl derived from the beta-lactone ring of the inhibitor. In the case of 1, nucleophilic addition to the beta-lactone ring is followed by addition of C-3O to the chloroethyl group, giving rise to a cyclic ether. The crystal structures were compared to that of the omuralide/CP structure solved previously, and the collective data provide new insights into the mechanism of inhibition and irreversible binding of 1. Upon opening of the beta-lactone ring, C-3O assumes the position occupied by a water molecule in the unligated enzyme and hinders deacylation of the enzyme-ligand complex. Furthermore, the resulting protonation state of Thr1NH2 deactivates the catalytic N-terminus.
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(as it appears on PubMed at http://www.pubmed.gov), where 16608349 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16608349}}
==About this Structure==
==About this Structure==
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[[Category: Proteasome]]
[[Category: Proteasome]]
[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:39:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:12:51 2008''

Revision as of 00:12, 28 July 2008

Image:2fak.png

Template:STRUCTURE 2fak

Crystal structure of Salinosporamide A in complex with the yeast 20S proteasome

Template:ABSTRACT PUBMED 16608349

About this Structure

2FAK is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding., Groll M, Huber R, Potts BC, J Am Chem Soc. 2006 Apr 19;128(15):5136-41. PMID:16608349

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