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2iu4

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|PDB= 2iu4 |SIZE=350|CAPTION= <scene name='initialview01'>2iu4</scene>, resolution 1.96&Aring;
|PDB= 2iu4 |SIZE=350|CAPTION= <scene name='initialview01'>2iu4</scene>, resolution 1.96&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HIQ:1-[1,2-DIHYDROXY-1-(HYDROXYMETHYL)ETHYL]-L-HISTIDINE'>HIQ</scene>
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|LIGAND= <scene name='pdbligand=HIQ:1-[1,2-DIHYDROXY-1-(HYDROXYMETHYL)ETHYL]-L-HISTIDINE'>HIQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu4 OCA], [http://www.ebi.ac.uk/pdbsum/2iu4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iu4 RCSB]</span>
}}
}}
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[[Category: Erni, B.]]
[[Category: Erni, B.]]
[[Category: Srinivas, A.]]
[[Category: Srinivas, A.]]
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[[Category: HIQ]]
 
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[[Category: SO4]]
 
[[Category: co-activator]]
[[Category: co-activator]]
[[Category: dihydroxyacetone]]
[[Category: dihydroxyacetone]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:33:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:48:42 2008''

Revision as of 00:48, 31 March 2008


PDB ID 2iu4

Drag the structure with the mouse to rotate
, resolution 1.96Å
Sites:
Ligands: ,
Activity: Glucokinase, with EC number 2.7.1.2
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ


Overview

Dihydroxyacetone (Dha) kinases are a novel family of kinases with signaling and metabolic functions. Here we report the x-ray structures of the transcriptional activator DhaS and the coactivator DhaQ and characterize their function. DhaQ is a paralog of the Dha binding Dha kinase subunit; DhaS belongs to the family of TetR repressors although, unlike all known members of this family, it is a transcriptional activator. DhaQ and DhaS form a stable complex that in the presence of Dha activates transcription of the Lactococcus lactis dha operon. Dha covalently binds to DhaQ through a hemiaminal bond with a histidine and thereby induces a conformational change, which is propagated to the surface via a cantilever-like structure. DhaS binding protects an inverted repeat whose sequence is GGACACATN6ATTTGTCC and renders two GC base pairs of the operator DNA hypersensitive to DNase I cleavage. The proximal half-site of the inverted repeat partially overlaps with the predicted -35 consensus sequence of the dha promoter.

About this Structure

2IU4 is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

Reference

Regulation of the Dha operon of Lactococcus lactis: a deviation from the rule followed by the Tetr family of transcription regulators., Christen S, Srinivas A, Bahler P, Zeller A, Pridmore D, Bieniossek C, Baumann U, Erni B, J Biol Chem. 2006 Aug 11;281(32):23129-37. Epub 2006 Jun 7. PMID:16760471

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