6w5e - Revision history

OCA at 14:17, 18 October 2023

2023-10-18T14:17:17Z

←Older revision		Revision as of 14:17, 18 October 2023
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	==Class D beta-lactamase BSU-2==		==Class D beta-lactamase BSU-2==
-	<StructureSection load='6w5e' size='340' side='right'caption='[[6w5e]]' scene=''>	+	<StructureSection load='6w5e' size='340' side='right'caption='[[6w5e]], [[Resolution\|resolution]] 1.30Å' 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=6W5E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6W5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6w5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W5E FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6w5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w5e OCA], [~~http~~://pdbe.org/6w5e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6w5e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6w5e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6w5e ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></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=6w5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w5e OCA], [https://pdbe.org/6w5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w5e RCSB], [https://www.ebi.ac.uk/pdbsum/6w5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w5e ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/YBXI_BACSU YBXI_BACSU]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The expression of beta-lactamases is a major mechanism of bacterial resistance to the beta-lactam antibiotics. Four molecular classes of beta-lactamases have been described (A, B, C and D), however until recently the class D enzymes were thought to exist only in Gram-negative bacteria. In the last few years, class D enzymes have been discovered in several species of Gram-positive microorganisms, such as Bacillus and Clostridia, and an investigation of their kinetic and structural properties has begun in earnest. Interestingly, it was observed that some species of Bacillus produce two distinct class D beta-lactamases, one highly active and the other with only basal catalytic activity. Analysis of amino acid sequences of active (BPU-1 from Bacillus pumilus) and inactive (BSU-2 from Bacillus subtilis and BAT-2 from Bacillus atrophaeus) enzymes suggests that presence of three additional amino acid residues in one of the surface loops of inefficient beta-lactamases may be responsible for their severely diminished activity. Our structural and docking studies show that the elongated loop of these enzymes severely restricts binding of substrates. Deletion of the three residues from the loops of BSU-2 and BAT-2 beta-lactamases relieves the steric hindrance and results in a significant increase in the catalytic activity of the enzymes. These data show that this surface loop plays an important role in modulation of the catalytic activity of Bacillus class D beta-lactamases.
		+
		+	A Surface Loop Modulates Activity of the Bacillus Class D beta-Lactamases.,Stewart NK, Bhattacharya M, Toth M, Smith CA, Vakulenko SB J Struct Biol. 2020 Jun 5:107544. doi: 10.1016/j.jsb.2020.107544. PMID:32512156<ref>PMID:32512156</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6w5e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus subtilis subsp. subtilis str. 168]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Smith CA]]		[[Category: Smith CA]]

OCA at 06:26, 25 June 2020

2020-06-25T06:26:41Z

←Older revision		Revision as of 06:26, 25 June 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6w5e ~~is ON HOLD until Paper Publication~~	+	==Class D beta-lactamase BSU-2==
-		+	<StructureSection load='6w5e' size='340' side='right'caption='[[6w5e]]' scene=''>
-	~~Authors~~: ~~Smith~~, C.A., ~~Vakulenko~~, S.B., ~~Stewart, N~~.K., ~~Toth, M~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W5E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W5E FirstGlance]. <br>
-	~~Description: Class D beta-lactamase BSU-2~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w5e OCA], [http://pdbe.org/6w5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w5e RCSB], [http://www.ebi.ac.uk/pdbsum/6w5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w5e ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Toth, M~~]]	+	__TOC__
-	[[Category: ~~Smith, C.A~~]]	+	</StructureSection>
-	[[Category: ~~Stewart, N.K~~]]	+	[[Category: Large Structures]]
-	[[Category: Vakulenko~~, S.B~~]]	+	[[Category: Smith CA]]
		+	[[Category: Stewart NK]]
		+	[[Category: Toth M]]
		+	[[Category: Vakulenko SB]]

OCA at 03:56, 13 May 2020

2020-05-13T03:56:59Z

←Older revision		Revision as of 03:56, 13 May 2020
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6w5e is ON HOLD	+	The entry 6w5e is ON HOLD until Paper Publication

	Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M.		Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M.

OCA: Protected "6w5e" [edit=sysop:move=sysop]

2020-03-27T08:22:51Z

Protected "6w5e" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:22, 27 March 2020

OCA: New page: '''Unreleased structure''' The entry 6w5e is ON HOLD Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M. Description: Class D beta-lactamase BSU-2 [[Category: Unreleased Str...

2020-03-27T08:22:50Z

New page: '''Unreleased structure''' The entry 6w5e is ON HOLD Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M. Description: Class D beta-lactamase BSU-2 [[Category: Unreleased Str...

New page

'''Unreleased structure'''

The entry 6w5e is ON HOLD

Authors: Smith, C.A., Vakulenko, S.B., Stewart, N.K., Toth, M.

Description: Class D beta-lactamase BSU-2
[[Category: Unreleased Structures]]
[[Category: Toth, M]]
[[Category: Smith, C.A]]
[[Category: Stewart, N.K]]
[[Category: Vakulenko, S.B]]