1dmh

[[Image:1dmh.gif|left|200px]]

|PDB= 1dmh |SIZE=350|CAPTION= <scene name='initialview01'>1dmh</scene>, resolution 1.7&Aring;

|SITE=

|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LIO:[1-PENTADECANOYL-2-DECANOYL-GLYCEROL-3-YL]PHOSPHONYL+CHOLINE'>LIO</scene>, <scene name='pdbligand=MCT:4-METHYLCATECHOL'>MCT</scene>

|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_1,2-dioxygenase Catechol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.1 1.13.11.1] </span>

|DOMAIN=

|RELATEDENTRY=[[1dlm|1DLM]], [[1dlq|1DLQ]], [[1dlt|1DLT]]

|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmh OCA], [http://www.ebi.ac.uk/pdbsum/1dmh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dmh RCSB]</span>

 

 

==Overview==

BACKGROUND: Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. Catechol 1,2-dioxygenases (1, 2-CTDs) have a rudimentary design structure - a homodimer with one catalytic non-heme ferric ion per monomer, that is (alphaFe(3+))(2). This is in contrast to the archetypical intradiol dioxygenase protocatechuate 3,4-dioxygenase (3,4-PCD), which forms more diverse oligomers, such as (alphabetaFe(3+))(2-12). RESULTS: The crystal structure of 1,2-CTD from Acinetobacter sp. ADP1 (Ac 1,2-CTD) was solved by single isomorphous replacement and refined to 2.0 A resolution. The structures of the enzyme complexed with catechol and 4-methylcatechol were also determined at resolutions of 1.9 A and 1.8 A, respectively. While the characteristics of the iron ligands are similar, Ac 1,2-CTD differs from 3,4-PCDs in that only one subunit is used to fashion each active-site cavity. In addition, a novel 'helical zipper', consisting of five N-terminal helices from each subunit, forms the molecular dimer axis. Two phospholipids were unexpectedly found to bind within an 8 x 35 A hydrophobic tunnel along this axis. CONCLUSIONS: The helical zipper domain of Ac 1, 2-CTD has no equivalent in other proteins of known structure. Sequence analysis suggests the domain is a common motif in all members of the 1,2-CTD family. Complexes with catechol and 4-methylcatechol are the highest resolution complex structures to date of an intradiol dioxygenase. Furthermore, they confirm several observations seen in 3,4-PCDs, including ligand displacement upon binding exogenous ligands. The structures presented here are the first of a new family of intradiol dioxygenases.

 

1DMH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMH OCA].

 

The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker., Vetting MW, Ohlendorf DH, Structure. 2000 Apr 15;8(4):429-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10801478 10801478]

[[Category: Acinetobacter sp.]]

[[Category: Catechol 1,2-dioxygenase]]

[[Category: Single protein]]

[[Category: Ohlendorf, D H.]]

[[Category: Vetting, M W.]]