2cbn
From Proteopedia
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| - | [[Image:2cbn.gif|left|200px]] | + | [[Image:2cbn.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF ZIPD FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 2cbn |SIZE=350|CAPTION= <scene name='initialview01'>2cbn</scene>, resolution 2.9Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_Z Ribonuclease Z], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.11 3.1.26.11] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF ZIPD FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CBN is a [ | + | 2CBN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CBN OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins., Kostelecky B, Pohl E, Vogel A, Schilling O, Meyer-Klaucke W, J Bacteriol. 2006 Feb;188(4):1607-14. PMID:[http:// | + | The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins., Kostelecky B, Pohl E, Vogel A, Schilling O, Meyer-Klaucke W, J Bacteriol. 2006 Feb;188(4):1607-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16452444 16452444] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribonuclease Z]] | [[Category: Ribonuclease Z]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:13:23 2008'' |
Revision as of 14:13, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Ribonuclease Z, with EC number 3.1.26.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ZIPD FROM ESCHERICHIA COLI
Overview
The elaC gene product from Escherichia coli, ZiPD, is a 3' tRNA-processing endonuclease belonging to the tRNase Z family of enzymes that have been identified in a wide variety of organisms. In contrast to the elaC homologue from Bacillus subtilis, E. coli elaC is not essential for viability, and although both enzymes process only precursor tRNA (pre-tRNA) lacking a CCA triplet at the 3' end in vitro, the physiological role of ZiPD remains enigmatic because all pre-tRNA species in E. coli are transcribed with the CCA triplet. We present the first crystal structure of ZiPD determined by multiple anomalous diffraction at a resolution of 2.9 A. This structure shares many features with the tRNase Z enzymes from B. subtilis and Thermotoga maritima, but there are distinct differences in metal binding and overall domain organization. Unlike the previously described homologous structures, ZiPD dimers display crystallographic symmetry and fully loaded metal sites. The ZiPD exosite is similar to that of the B. subtilis enzyme structurally, but its position with respect to the protein core differs substantially, illustrating its ability to act as a clamp in binding tRNA. Furthermore, the ZiPD crystal structure presented here provides insight into the enzyme's cooperativity and assists the ongoing attempt to elucidate the physiological function of this protein.
About this Structure
2CBN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins., Kostelecky B, Pohl E, Vogel A, Schilling O, Meyer-Klaucke W, J Bacteriol. 2006 Feb;188(4):1607-14. PMID:16452444
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