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2bum

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[[Image:2bum.gif|left|200px]]<br /><applet load="2bum" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bum.gif|left|200px]]
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caption="2bum, resolution 1.80&Aring;" />
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'''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1'''<br />
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{{Structure
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|PDB= 2bum |SIZE=350|CAPTION= <scene name='initialview01'>2bum</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=HYD:HYDROXY GROUP'>HYD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BUM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] and [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=HYD:'>HYD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] Known structural/functional Site: <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUM OCA].
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2BUM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] and [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUM OCA].
==Reference==
==Reference==
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Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15487948 15487948]
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Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15487948 15487948]
[[Category: Acinetobacter calcoaceticus]]
[[Category: Acinetobacter calcoaceticus]]
[[Category: Acinetobacter sp.]]
[[Category: Acinetobacter sp.]]
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[[Category: non-heme iron]]
[[Category: non-heme iron]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:55 2008''

Revision as of 14:06, 20 March 2008

Image:2bum.gif


PDB ID 2bum

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: and
Activity: Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1


Overview

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

About this Structure

2BUM is a Protein complex structure of sequences from Acinetobacter calcoaceticus and Acinetobacter sp.. Full crystallographic information is available from OCA.

Reference

Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:15487948

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