1zrr
From Proteopedia
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| - | [[Image:1zrr.gif|left|200px]] | + | [[Image:1zrr.gif|left|200px]] |
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| - | '''Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella''' | + | {{Structure |
| + | |PDB= 1zrr |SIZE=350|CAPTION= <scene name='initialview01'>1zrr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZRR is a [ | + | 1ZRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. This structure supersedes the now removed PDB entry 1M4O. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRR OCA]. |
==Reference== | ==Reference== | ||
| - | A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings., Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J, J Biomol NMR. 2006 Feb;34(2):117-27. PMID:[http:// | + | A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings., Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J, J Biomol NMR. 2006 Feb;34(2):117-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16518698 16518698] |
[[Category: Klebsiella oxytoca]] | [[Category: Klebsiella oxytoca]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nickel]] | [[Category: nickel]] | ||
| - | ''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 15:39:03 2008'' |
Revision as of 13:39, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella
Overview
Acireductone dioxygenase (ARD) from Klebsiella ATCC 8724 is a metalloenzyme that is capable of catalyzing different reactions with the same substrates (acireductone and O2) depending upon the metal bound in the active site. A model for the solution structure of the paramagnetic Ni2+-containing ARD has been refined using residual dipolar couplings (RDCs) measured in two media. Additional dihedral restraints based on chemical shift (TALOS) were included in the refinement, and backbone structure in the vicinity of the active site was modeled from a crystallographic structure of the mouse homolog of ARD. The incorporation of residual dipolar couplings into the structural refinement alters the relative orientations of several structural features significantly, and improves local secondary structure determination. Comparisons between the solution structures obtained with and without RDCs are made, and structural similarities and differences between mouse and bacterial enzymes are described. Finally, the biological significance of these differences is considered.
About this Structure
1ZRR is a Single protein structure of sequence from Klebsiella oxytoca. This structure supersedes the now removed PDB entry 1M4O. Full crystallographic information is available from OCA.
Reference
A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings., Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J, J Biomol NMR. 2006 Feb;34(2):117-27. PMID:16518698
Page seeded by OCA on Thu Mar 20 15:39:03 2008
Categories: Klebsiella oxytoca | Single protein | Hoefler, C. | Ju, T. | Liang, J. | Pochapsky, S S. | Pochapsky, T C. | NI | Beta helix | Cupin | Methionine salvage | Nickel
