1bc2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(21 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1bc2.gif|left|200px]]<br />
<applet load="1bc2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bc2, resolution 1.9&Aring;" />
'''ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''<br />


==Overview==
==ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS==
The structure of the zinc-dependent beta-lactamase II from Bacillus cereus, has been determined at 1.9 A resolution in a crystal form with two, molecules in the asymmetric unit and 400 waters (space group P3121; Rcryst, = 20.8%). The active site contains two zinc ions: Zn1 is tightly, coordinated by His86, His88, and His149, while Zn2 is loosely coordinated, by Asp90, Cys168, and His210. A water molecule (W1) lies between the two, zinc ions but is significantly closer to Zn1 and at a distance of only 1.9, A is effectively a hydroxide moiety and a potential, preactivated, nucleophile. In fact, Asp90 bridges W1 to Zn2, and its location is thus, distinct from that of the bridging water molecules in the binuclear zinc, peptidases or other binuclear zinc hydrolases. Modeling of penicillin, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9730812 (full description)]]
<StructureSection load='1bc2' size='340' side='right'caption='[[1bc2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC2 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1bc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc2 OCA], [https://pdbe.org/1bc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds.
== 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/bc/1bc2_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=1bc2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BC2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: ASA, ASB, ZNA and ZNB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BC2 OCA]].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme., Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ, Biochemistry. 1998 Sep 8;37(36):12404-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9730812 9730812]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Fabiane SM]]
[[Category: Fabiane, S.M.]]
[[Category: Sutton BJ]]
[[Category: Sutton, B.J.]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: antibiotic resistance]]
[[Category: hydrolase]]
[[Category: metallo beta-lactamase]]
[[Category: penicillinase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:20:12 2007''

Latest revision as of 09:35, 7 February 2024

ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUSZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS

Structural highlights

1bc2 is a 2 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLA2_BACCE Can hydrolyze carbapenem compounds.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1bc2, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1bc2&oldid=4040493"