1mxs
From Proteopedia
(New page: 200px<br /><applet load="1mxs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxs, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1mxs.gif|left|200px]]<br /><applet load="1mxs" size=" | + | [[Image:1mxs.gif|left|200px]]<br /><applet load="1mxs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mxs, resolution 2.20Å" /> | caption="1mxs, resolution 2.20Å" /> | ||
'''Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.'''<br /> | '''Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida | + | 2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is a key enzyme in the Entner-Doudoroff pathway which catalyses the cleavage of KDPG via a class I Schiff-base mechanism. The crystal structure of this enzyme has been refined to a crystallographic residual R = 17.1% (R(free) = 21.4%). The N-terminal helix caps one side of the torus of the (betaalpha)(8)-barrel and the active site is located on the opposite, carboxylic side of the barrel. The Schiff-base-forming Lys145 is coordinated by a sulfate (or phosphate) ion and two solvent water molecules. The interactions that stabilize the trimer are predominantly hydrophobic, with the exception of the cyclically permuted bonds formed between Glu132 OE1 of one molecule and Thr129 OG1 of a symmetry-equivalent molecule. Except for the N-terminal helix, the structure of KDPG aldolase from P. putida closely resembles the structure of the homologous enzyme from Escherichia coli. |
==About this Structure== | ==About this Structure== | ||
| - | 1MXS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14] Full crystallographic information is available from [http:// | + | 1MXS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arni, R | + | [[Category: Arni, R K.]] |
| - | [[Category: Bell, B | + | [[Category: Bell, B J.]] |
[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
| - | [[Category: Rios-Steiner, J | + | [[Category: Rios-Steiner, J L.]] |
[[Category: Tulinsky, A.]] | [[Category: Tulinsky, A.]] | ||
[[Category: Watanabe, L.]] | [[Category: Watanabe, L.]] | ||
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[[Category: sulfate]] | [[Category: sulfate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:14 2008'' |
Revision as of 12:00, 21 February 2008
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Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.
Overview
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is a key enzyme in the Entner-Doudoroff pathway which catalyses the cleavage of KDPG via a class I Schiff-base mechanism. The crystal structure of this enzyme has been refined to a crystallographic residual R = 17.1% (R(free) = 21.4%). The N-terminal helix caps one side of the torus of the (betaalpha)(8)-barrel and the active site is located on the opposite, carboxylic side of the barrel. The Schiff-base-forming Lys145 is coordinated by a sulfate (or phosphate) ion and two solvent water molecules. The interactions that stabilize the trimer are predominantly hydrophobic, with the exception of the cyclically permuted bonds formed between Glu132 OE1 of one molecule and Thr129 OG1 of a symmetry-equivalent molecule. Except for the N-terminal helix, the structure of KDPG aldolase from P. putida closely resembles the structure of the homologous enzyme from Escherichia coli.
About this Structure
1MXS is a Single protein structure of sequence from Pseudomonas putida with as ligand. Active as 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 Full crystallographic information is available from OCA.
Reference
Structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida., Bell BJ, Watanabe L, Rios-Steiner JL, Tulinsky A, Lebioda L, Arni RK, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1454-8. Epub 2003, Jul 23. PMID:12876349
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