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[[Image:2fff.gif|left|200px]]
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{{STRUCTURE_2fff|  PDB=2fff  |  SCENE=  }}
'''Open Form of a Class A Transpeptidase Domain'''


==Open Form of a Class A Transpeptidase Domain==
<StructureSection load='2fff' size='340' side='right'caption='[[2fff]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fff]] is a 2 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=2FFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FFF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=2fff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fff OCA], [https://pdbe.org/2fff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fff RCSB], [https://www.ebi.ac.uk/pdbsum/2fff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fff ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O70038_STREE O70038_STREE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/2fff_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2fff ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.


==Overview==
Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae.,Lovering AL, De Castro L, Lim D, Strynadka NC Protein Sci. 2006 Jul;15(7):1701-9. Epub 2006 Jun 2. PMID:16751607<ref>PMID:16751607</ref>
The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2FFF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFF OCA].
</div>
<div class="pdbe-citations 2fff" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae., Lovering AL, De Castro L, Lim D, Strynadka NC, Protein Sci. 2006 Jul;15(7):1701-9. Epub 2006 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16751607 16751607]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
[[Category: Lovering, A L.]]
[[Category: Lovering AL]]
[[Category: Strynadka, N C.J.]]
[[Category: Strynadka NCJ]]
[[Category: Transpeptidase fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:49:51 2008''

Latest revision as of 09:26, 30 August 2023

Open Form of a Class A Transpeptidase Domain

2fff, resolution 2.23Å

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