This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3pnl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:3pnl.png|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3pnl", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3pnl| PDB=3pnl | SCENE= }} | {{STRUCTURE_3pnl| PDB=3pnl | SCENE= }} | ||
| - | |||
===Crystal Structure of E.coli Dha kinase DhaK-DhaL complex=== | ===Crystal Structure of E.coli Dha kinase DhaK-DhaL complex=== | ||
| + | {{ABSTRACT_PUBMED_21209328}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/DHAK_ECOLI DHAK_ECOLI]] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone. [[http://www.uniprot.org/uniprot/DHAL_ECOLI DHAL_ECOLI]] ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaL-ADP receives a phosphoryl group from DhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of DhaR. DhaL-ATP is inactive. | |
| - | + | ||
| - | + | ||
| - | -- | + | |
| - | + | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3pnl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli | + | [[3pnl]] is a 2 chain structure with 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=3PNL OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021209328</ref><references group="xtra"/><references/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Escherichia coli k-12]] | ||
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | ||
[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
| Line 31: | Line 18: | ||
[[Category: McDonald, L.]] | [[Category: McDonald, L.]] | ||
[[Category: Shi, R.]] | [[Category: Shi, R.]] | ||
| + | [[Category: Bsgi]] | ||
| + | [[Category: Dha kinase]] | ||
| + | [[Category: Montreal-kingston bacterial structural genomics initiative]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 08:17, 8 May 2013
Contents |
Crystal Structure of E.coli Dha kinase DhaK-DhaL complex
Template:ABSTRACT PUBMED 21209328
Function
[DHAK_ECOLI] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone. [DHAL_ECOLI] ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaL-ADP receives a phosphoryl group from DhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of DhaR. DhaL-ATP is inactive.
About this Structure
3pnl is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Shi R, McDonald L, Cui Q, Matte A, Cygler M, Ekiel I. Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase. Proc Natl Acad Sci U S A. 2011 Jan 5. PMID:21209328 doi:10.1073/pnas.1012596108
