3pnm: Difference between revisions
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{{STRUCTURE_3pnm| PDB=3pnm | SCENE= }} | {{STRUCTURE_3pnm| PDB=3pnm | SCENE= }} | ||
===Crystal Structure of E.coli Dha kinase DhaK (H56A)=== | ===Crystal Structure of E.coli Dha kinase DhaK (H56A)=== | ||
{{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. | |||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021209328</ref><references group="xtra"/><references/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] | ||
| Line 30: | Line 18: | ||
[[Category: McDonald, L.]] | [[Category: McDonald, L.]] | ||
[[Category: Shi, R.]] | [[Category: Shi, R.]] | ||
[[Category: Bsgi]] | |||
[[Category: Montreal-kingston bacterial structural genomics initiative]] | |||
[[Category: Structural genomic]] | |||
[[Category: Transferase]] | |||
Revision as of 08:23, 8 May 2013
Crystal Structure of E.coli Dha kinase DhaK (H56A)
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.
About this Structure
3pnm is a 4 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
