1jtd

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[[Image:1jtd.gif|left|200px]]
 
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{{Structure
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==Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase==
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|PDB= 1jtd |SIZE=350|CAPTION= <scene name='initialview01'>1jtd</scene>, resolution 2.30&Aring;
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<StructureSection load='1jtd' size='340' side='right'caption='[[1jtd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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<table><tr><td colspan='2'>[[1jtd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JTD FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtd OCA], [https://pdbe.org/1jtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jtd RCSB], [https://www.ebi.ac.uk/pdbsum/1jtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jtd ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtd OCA], [http://www.ebi.ac.uk/pdbsum/1jtd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jtd RCSB]</span>
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== Function ==
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}}
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[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jt/1jtd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jtd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.
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'''Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase'''
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Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase.,Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC Nat Struct Biol. 2001 Oct;8(10):848-52. PMID:11573088<ref>PMID:11573088</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1jtd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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*[[TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)|TEM1-beta-Lactamase/beta-lactamase Inhibitor Protein (BLIP)]]
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==About this Structure==
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== References ==
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1JTD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTD OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase., Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC, Nat Struct Biol. 2001 Oct;8(10):848-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11573088 11573088]
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[[Category: Beta-lactamase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Streptomyces exfoliatus]]
[[Category: Streptomyces exfoliatus]]
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[[Category: Castro, L De.]]
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[[Category: De Castro L]]
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[[Category: Jensen, S.]]
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[[Category: Jensen S]]
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[[Category: Kang, S G.]]
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[[Category: Kang SG]]
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[[Category: Lee, H S.]]
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[[Category: Lee HS]]
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[[Category: Lee, K J.]]
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[[Category: Lee KJ]]
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[[Category: Lim, D C.]]
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[[Category: Lim DC]]
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[[Category: Park, H U.]]
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[[Category: Park HU]]
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[[Category: Strynadka, N C.J.]]
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[[Category: Strynadka NCJ]]
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[[Category: beta-lactamase inhibitor protein-ii]]
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[[Category: blip-ii]]
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[[Category: protein-protein complex]]
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[[Category: tem-1 beta-lactamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:42 2008''
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Current revision

Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase

PDB ID 1jtd

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