7xf9
From Proteopedia
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==Crystal structure of human bleomycin hydrolase H372A mutant== | ==Crystal structure of human bleomycin hydrolase H372A mutant== | ||
| - | <StructureSection load='7xf9' size='340' side='right'caption='[[7xf9]]' scene=''> | + | <StructureSection load='7xf9' size='340' side='right'caption='[[7xf9]], [[Resolution|resolution]] 3.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XF9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7xf9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XF9 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xf9 OCA], [https://pdbe.org/7xf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7xf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xf9 ProSAT]</span></td></tr> | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xf9 OCA], [https://pdbe.org/7xf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7xf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xf9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/BLMH_HUMAN BLMH_HUMAN]] The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human bleomycin hydrolase (hBH) catalyzes deamidation of the anticancer drug bleomycins (BLM). This enzyme is involved in BLM detoxification and drug resistance. Herein, we report the putative BLM-binding site and catalytic mechanism of hBH. The crystal structures and biochemical studies suggest that hBH cleaves its C-terminal residue without significant preference for the type of amino acid, and therefore can accordingly accommodate the beta-aminoalanine amide moiety of BLM for deamidation. Interestingly, hBH is capable of switching from a cysteine protease to a serine protease that is unable to cleave the secondary amide of hBH C-terminus but reacts with the primary amide of BLMs. | ||
| + | |||
| + | The Structure-Function Relationship of Human Bleomycin Hydrolase: Mutation of a Cysteine Protease into a Serine Protease.,Zheng YZ, Cui J, Wang YL, Huang SJ, Lin EC, Huang SC, Rudolf JD, Yan X, Chang CY Chembiochem. 2022 Jun 20;23(12):e202200186. doi: 10.1002/cbic.202200186. Epub, 2022 May 5. PMID:35467071<ref>PMID:35467071</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7xf9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bleomycin hydrolase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chang, | + | [[Category: Chang, C Y]] |
| + | [[Category: Huang, S J]] | ||
| + | [[Category: Lin, E C]] | ||
| + | [[Category: Toh, S I]] | ||
| + | [[Category: Wang, Y L]] | ||
| + | [[Category: Zheng, Y Z]] | ||
| + | [[Category: Cysteine protease]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 16:27, 6 July 2022
Crystal structure of human bleomycin hydrolase H372A mutant
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