1ef0: Difference between revisions
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|PDB= 1ef0 |SIZE=350|CAPTION= <scene name='initialview01'>1ef0</scene>, resolution 2.1Å | |PDB= 1ef0 |SIZE=350|CAPTION= <scene name='initialview01'>1ef0</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef0 OCA], [http://www.ebi.ac.uk/pdbsum/1ef0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ef0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
[[Category: Xu, M Q.]] | [[Category: Xu, M Q.]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: mini-precursor]] | [[Category: mini-precursor]] | ||
[[Category: protein splicing]] | [[Category: protein splicing]] | ||
''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 20:01:13 2008'' | ||
Revision as of 20:01, 30 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PI-SCEI MINIPRECURSOR
OverviewOverview
PI-SceI is a member of a class of proteins (inteins) that excise themselves from a precursor protein and in the process ligate the flanking protein sequences (exteins). We report here the 2.1-A resolution crystal structure of a PI-SceI miniprecursor (VMA29) containing 10 N-terminal extein residues and 4 C-terminal extein residues. Mutations at the N- and C-terminal splicing junctions, blocking in vivo protein splicing, allowed the miniprecursor to be purified and crystallized. The structure reveals both the N- and C-terminal scissile peptide bonds to be in distorted trans conformations (tau approximately 100 degrees ). Modeling of the wild-type PI-SceI based on the VMA29 structure indicates a large conformational change (movement of >9 A) must occur to allow transesterification to be completed. A zinc atom was discovered at the C-terminal splicing junction. Residues Cys(455), His(453), and Glu(80) along with a water molecule (Wat(53)) chelate the zinc atom. The crystal structure of VMA29 has captured the intein in its pre-spliced state.
About this StructureAbout this Structure
1EF0 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the protein splicing mechanism of PI-SceI., Poland BW, Xu MQ, Quiocho FA, J Biol Chem. 2000 Jun 2;275(22):16408-13. PMID:10828056
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