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.

3sw8

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Strep Peptide Deformylase with a time dependent dichlorobenzamide-reverse hydroxamic acid

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sw8"

Categories: Large Structures | Streptococcus pneumoniae | Campobasso N | Smith KJ

@@ Line 3: / Line 3: @@
 <StructureSection load='3sw8' size='340' side='right'caption='[[3sw8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sw8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SW8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sw8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SW8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5LI:2,3-DICHLORO-N-{2-[FORMYL(HYDROXY)AMINO]ETHYL}BENZAMIDE'>5LI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.702&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3str|3str]], [[3svj|3svj]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5LI:2,3-DICHLORO-N-{2-[FORMYL(HYDROXY)AMINO]ETHYL}BENZAMIDE'>5LI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">defB, def3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=3sw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sw8 OCA], [https://pdbe.org/3sw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sw8 RCSB], [https://www.ebi.ac.uk/pdbsum/3sw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sw8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/Q939R9_STREE Q939R9_STREE]] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).[HAMAP-Rule:MF_00163]
+[https://www.uniprot.org/uniprot/Q939R9_STREE Q939R9_STREE] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).[HAMAP-Rule:MF_00163]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The continual bacterial adaptation to antibiotics creates an ongoing medical need for the development of novel therapeutics. Polypeptide deformylase (PDF) is a highly conserved bacterial enzyme, which is essential for viability. It has previously been shown that PDF inhibitors represent a promising new area for the development of antimicrobial agents, and that many of the best PDF inhibitors demonstrate slow, time dependent binding. In order to gain a better understanding of the mechanistic origin of this time dependent inhibition, we examined in detail the kinetics of PDF catalysis and inhibition by several different PDF inhibitors. Varying pH and solvent isotope led to clear changes in time dependent inhibition parameters, as did inclusion of NaCl, which binds to the active site metal of PDF. Quantitative analysis of these results demonstrated that the observed time dependence arises from slow binding of the inhibitors to the active site metal. However, we also found several metal binding inhibitors that displayed rapid, non-time dependent onset of inhibition. By a combination of structural and chemical modification studies, we show that metal binding is only slow when the rest of the inhibitor makes optimal hydrogen bonds within the subsites of PDF. Both of these interactions between the inhibitor and enzyme were found to be necessary to observe time dependent inhibition, as elimination of either leads to its loss.
-Understanding the Origins of Time Dependent Inhibition by Polypeptide Deformylase Inhibitors.,Totoritis R, Duraiswami C, Taylor AN, Kerrigan JJ, Campobasso N, Ward P, King BW, Murray-Thompson MF, Jones AD, Van Aller G, Aubart KM, Zalacain M, Thrall SH, Meek TD, Schwartz B Biochemistry. 2011 Jun 28. PMID:21711014<ref>PMID:21711014</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3sw8" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Peptide deformylase]]
+[[Category: Streptococcus pneumoniae]]
-[[Category: Campobasso, N]]
+[[Category: Campobasso N]]
-[[Category: Smith, K J]]
+[[Category: Smith KJ]]
-[[Category: Alpha-beta]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Metal binding protein]]

3sw8

From Proteopedia

Current revision

Strep Peptide Deformylase with a time dependent dichlorobenzamide-reverse hydroxamic acid

Structural highlights

Function

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox