1mi8: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi8 OCA], [http://www.ebi.ac.uk/pdbsum/1mi8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mi8 RCSB]</span> | |||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:24 2008'' | ||
Revision as of 22:16, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.0 Angstrom crystal structure of a DnaB intein from Synechocystis sp. PCC 6803
OverviewOverview
We have determined the crystal structure of a 154-residue intein derived from the dnaB gene of Synechocystis sp. strain PCC6803 and refined it to a 2.0-A resolution. The x-ray structure suggests that this intein possesses two catalytic sites that appear to be separately responsible for splicing and cleavage of the N- and C-terminal scissile bonds. The conserved intein block F residues are the important components of a catalytic site for side chain cyclization of the last intein residue, Asn-154. The data suggest that the imidazole ring of His-143 is involved in the activation of the side chain Ndelta atom of Asn-154, leading to a nucleophilic attack on the carbonyl carbon of Asn-154. Substitution of His-143 with Ala or Gln resulted in the inhibition of C-terminal cleavage. His-153, Asp-136, and a water molecule appear to constitute an oxyanion binding site by contacting the carbonyl oxygen of Asn-154 to stabilize the transition state. The structure and mutagenesis data also support that the close contact between the hydroxyl groups of Thr-138 and Ser-155, whose side chain participates in an S --> O acyl shift, plays an important role in the nucleophile orientation. Our structural modeling suggests that this catalytic module is conserved in the C-terminal subdomains of inteins from diverse organisms.
About this StructureAbout this Structure
1MI8 is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing., Ding Y, Xu MQ, Ghosh I, Chen X, Ferrandon S, Lesage G, Rao Z, J Biol Chem. 2003 Oct 3;278(40):39133-42. Epub 2003 Jul 23. PMID:12878593
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