This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2c81

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:31, 11 September 2015

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

Structural highlights

2c81 is a 1 chain structure with sequence from Atcc 24. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GLDSA_BACCI] Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (DOI) to form 2-deoxy-scyllo-inosamine (DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI) into 2-deoxystreptamine (DOS). Is also able to catalyze the transamination of scyllo-inosose to form scyllo-inosamine, although this reaction may be not physiological.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tamegai H, Nango E, Kuwahara M, Yamamoto H, Ota Y, Kuriki H, Eguchi T, Kakinuma K. Identification of L-glutamine: 2-deoxy-scyllo-inosose aminotransferase required for the biosynthesis of butirosin in Bacillus circulans. J Antibiot (Tokyo). 2002 Aug;55(8):707-14. PMID:12374384
↑ Huang F, Li Y, Yu J, Spencer JB. Biosynthesis of aminoglycoside antibiotics: cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine. Chem Commun (Camb). 2002 Dec 7;(23):2860-1. PMID:12478783
↑ Yokoyama K, Kudo F, Kuwahara M, Inomata K, Tamegai H, Eguchi T, Kakinuma K. Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis. J Am Chem Soc. 2005 Apr 27;127(16):5869-74. PMID:15839685 doi:http://dx.doi.org/10.1021/ja0445948
↑ Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB. Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis. Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611 doi:10.1002/prot.21076

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c81"

@@ Line 2: / Line 2: @@
 <StructureSection load='2c81' size='340' side='right' caption='[[2c81]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c81]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C81 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c81]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_24 Atcc 24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C81 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C81 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c81 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c81 RCSB], [http://www.ebi.ac.uk/pdbsum/2c81 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c81 OCA], [http://pdbe.org/2c81 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c81 RCSB], [http://www.ebi.ac.uk/pdbsum/2c81 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GLDSA_BACCI GLDSA_BACCI]] Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (DOI) to form 2-deoxy-scyllo-inosamine (DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI) into 2-deoxystreptamine (DOS). Is also able to catalyze the transamination of scyllo-inosose to form scyllo-inosamine, although this reaction may be not physiological.<ref>PMID:12374384</ref> <ref>PMID:12478783</ref> <ref>PMID:15839685</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 24: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c81" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus circulans]]
+[[Category: Atcc 24]]
 [[Category: Blundell, T L]]
 [[Category: Chirgadze, D Y]]

2c81

From Proteopedia

Revision as of 16:31, 11 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox