4rx2: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis==

~~The entry~~ 4rx2 is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4rx2]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX2 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RX2 FirstGlance].

~~Authors~~: ~~Stojanoski~~, V.~~, Chow, D~~., ~~Hu, L~~.~~, Sankaran, B~~.~~, Gilbert, H~~., ~~Prasad, B~~.V.V., ~~Palzkill, T~~.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[4rva|4rva]]</td></tr>

~~Description~~: ~~A triple mutant~~ in the ~~omega~~-~~loop~~ of TEM-1 beta-lactamase ~~changes the substrate profile via a large conformational change and an altered general base for catalysis~~

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rx2 RCSB], [http://www.ebi.ac.uk/pdbsum/4rx2 PDBsum]</td></tr>

[[Category: ~~Stojanoski~~, V]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

__TOC__

</StructureSection>

[[Category: Beta-lactamase]]

[[Category: Chow, D]]

[[Category: Gilbert, H]]

[[Category: Hu, L]]

[[Category: Palzkill, T]]

[[Category: Prasad, B V.V]]

[[Category: Sankaran, B]]

[[Category: ~~Gilbert~~, H]]

[[Category: Stojanoski, V]]

[[Category: ~~Chow, D~~]]

[[Category: Globular]]

[[Category: ~~Hu, L]]~~

[[Category: Hydrolase]]

~~[[Category: Prasad, B.V.V~~]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis==
+<StructureSection load='4rx2' size='340' side='right' caption='[[4rx2]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
-The entry 4rx2 is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4rx2]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RX2 FirstGlance]. <br>
-Authors: Stojanoski, V., Chow, D., Hu, L., Sankaran, B., Gilbert, H., Prasad, B.V.V., Palzkill, T.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[4rva|4rva]]</td></tr>
-Description: A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
-[[Category: Unreleased Structures]]
+<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=4rx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rx2 RCSB], [http://www.ebi.ac.uk/pdbsum/4rx2 PDBsum]</span></td></tr>
-[[Category: Stojanoski, V]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
+__TOC__
+</StructureSection>
+[[Category: Beta-lactamase]]
+[[Category: Chow, D]]
+[[Category: Gilbert, H]]
+[[Category: Hu, L]]
 [[Category: Palzkill, T]]
+[[Category: Prasad, B V.V]]
 [[Category: Sankaran, B]]
-[[Category: Gilbert, H]]
+[[Category: Stojanoski, V]]
-[[Category: Chow, D]]
+[[Category: Globular]]
-[[Category: Hu, L]]
+[[Category: Hydrolase]]
-[[Category: Prasad, B.V.V]]