2zak
From Proteopedia
(New page: 200px {{Structure |PDB= 2zak |SIZE=350|CAPTION= <scene name='initialview01'>2zak</scene>, resolution 2.01Å |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+F...) |
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|GENE= ybiK (iaaA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ybiK (iaaA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04701 Asparaginase_2]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04701 Asparaginase_2]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zak OCA], [http://www.ebi.ac.uk/pdbsum/2zak PDBsum | + | |RELATEDENTRY=[[1k2x|1K2X]], [[1jn9|1JN9]], [[1t3m|1T3M]], [[1seo|1SEO]], [[2gez|2GEZ]], [[2gac|2GAC]], [[9gac|9GAC]], [[9gaf|9GAF]], [[9gaa|9GAA]], [[1p4v|1P4V]] |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zak OCA], [http://www.ebi.ac.uk/pdbsum/2zak PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zak RCSB]</span> | ||
}} | }} | ||
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[[Category: precursor]] | [[Category: precursor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:19:55 2008'' |
Revision as of 02:19, 31 March 2008
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| , resolution 2.01Å | |||||||
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| Sites: | , , , and | ||||||
| Ligands: | , , | ||||||
| Gene: | ybiK (iaaA) (Escherichia coli) | ||||||
| Domains: | Asparaginase_2 | ||||||
| Related: | 1K2X, 1JN9, 1T3M, 1SEO, 2GEZ, 2GAC, 9GAC, 9GAF, 9GAA, 1P4V
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Orthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation
Overview
Plant-type L-asparaginases hydrolyze the side-chain amide bond of L-asparagine or its beta-peptides. They belong to the N-terminal nucleophile (Ntn) hydrolases and are synthesized as inactive precursor molecules. Activation occurs via the autoproteolytic release of two subunits, alpha and beta, the latter of which carries the nucleophile at its N-terminus. Crystallographic studies of plant-type asparaginases have focused on an Escherichia coli homologue (EcAIII), which has been crystallized in several crystal forms. Although they all belong to the same P2(1)2(1)2(1) space group with similar unit-cell parameters, they display different crystal-packing arrangements and thus should be classified as separate polymorphs. This variability stems mainly from different positions of the EcAIII molecules within the unit cell, although they also exhibit slight differences in orientation. The intermolecular interactions that trigger different crystal lattice formation are mediated by ions, which represent the most variable component of the crystallization conditions. This behaviour confirms recent observations that small molecules might promote protein crystal lattice formation.
About this Structure
2ZAK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal packing of plant-type L-asparaginase from Escherichia coli., Michalska K, Borek D, Hernandez-Santoyo A, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):309-20. Epub 2008, Feb 20. PMID:18323626
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