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.
4cxr
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Mycobaterium tuberculosis transaminase BioA complexed with 1-(1,3- benzothiazol-2-yl)methanamine== | |
| - | + | <StructureSection load='4cxr' size='340' side='right' caption='[[4cxr]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4cxr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4mqo 4mqo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CXR FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2BG:1-(1,3-BENZOTHIAZOL-2-YL)METHANAMINE'>2BG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cxq|4cxq]], [[4mqp|4mqp]], [[4mqq|4mqq]], [[4mqr|4mqr]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylmethionine--8-amino-7-oxononanoate_transaminase Adenosylmethionine--8-amino-7-oxononanoate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.62 2.6.1.62] </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=4cxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cxr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cxr RCSB], [http://www.ebi.ac.uk/pdbsum/4cxr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/BIOA_MYCTU BIOA_MYCTU]] Catalyzes the reversible transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. Can also use sinefungin as substrate.<ref>PMID:16984394</ref> | [[http://www.uniprot.org/uniprot/BIOA_MYCTU BIOA_MYCTU]] Catalyzes the reversible transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. Can also use sinefungin as substrate.<ref>PMID:16984394</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 7,8-Diaminopelargonic acid synthase (BioA) of Mycobacterium tuberculosis is a recently validated target for therapeutic intervention in the treatment of tuberculosis (TB). Using biophysical fragment screening and structural characterization of compounds, we have identified a potent aryl hydrazine inhibitor of BioA that reversibly modifies the pyridoxal-5'-phosphate (PLP) cofactor, forming a stable quinonoid. Analogous hydrazides also form covalent adducts that can be observed crystallographically but are incapable of inactivating the enzyme. In the X-ray crystal structures, small molecules induce unexpected conformational remodeling in the substrate binding site. We compared these conformational changes to those induced upon binding of the substrate (7-keto-8-aminopelargonic acid), and characterized the inhibition kinetics and the X-ray crystal structures of BioA with the hydrazine compound and analogues to unveil the mechanism of this reversible covalent modification. | ||
| - | + | Inhibition of Mycobacterium tuberculosis Transaminase BioA by Aryl Hydrazines and Hydrazides.,Dai R, Wilson DJ, Geders TW, Aldrich CC, Finzel BC Chembiochem. 2014 Mar 3;15(4):575-86. doi: 10.1002/cbic.201300748. Epub 2014 Jan , 31. PMID:24482078<ref>PMID:24482078</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Adenosylmethionine--8-amino-7-oxononanoate transaminase]] | [[Category: Adenosylmethionine--8-amino-7-oxononanoate transaminase]] | ||
| - | [[Category: Dai, R | + | [[Category: Dai, R]] |
| - | [[Category: Finzel, B C | + | [[Category: Finzel, B C]] |
| - | [[Category: Geders, T W | + | [[Category: Geders, T W]] |
[[Category: Plp]] | [[Category: Plp]] | ||
[[Category: Transaminase]] | [[Category: Transaminase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Tuberculosis]] | [[Category: Tuberculosis]] | ||
Revision as of 14:04, 24 December 2014
Mycobaterium tuberculosis transaminase BioA complexed with 1-(1,3- benzothiazol-2-yl)methanamine
| |||||||||||
