2c81

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[[Image:2c81.gif|left|200px]]<br /><applet load="2c81" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c81.gif|left|200px]]
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caption="2c81, resolution 1.70&Aring;" />
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'''CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.'''<br />
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{{Structure
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|PDB= 2c81 |SIZE=350|CAPTION= <scene name='initialview01'>2c81</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Pmp+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PMP:4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE'>PMP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with <scene name='pdbligand=PMP:'>PMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Pmp+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C81 OCA].
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2C81 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C81 OCA].
==Reference==
==Reference==
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Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis., Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB, Proteins. 2006 Oct 1;65(1):220-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16894611 16894611]
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Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis., Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB, Proteins. 2006 Oct 1;65(1):220-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16894611 16894611]
[[Category: Bacillus circulans]]
[[Category: Bacillus circulans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Tang, X.]]
[[Category: Tang, X.]]
[[Category: PMP]]
[[Category: PMP]]
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[[Category: aminoglycoside antibiotics]]
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[[Category: aminoglycoside antibiotic]]
[[Category: aminotransferase]]
[[Category: aminotransferase]]
[[Category: butirosin]]
[[Category: butirosin]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:03 2008''

Revision as of 14:12, 20 March 2008


PDB ID 2c81

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, resolution 1.70Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.


Overview

The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.

About this Structure

2C81 is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis., Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB, Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611

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