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.


1shv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1shv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1shv, resolution 1.98&Aring;" /> '''STRUCTURE OF SHV-1 B...)
Current revision (06:17, 23 August 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1shv.jpg|left|200px]]<br /><applet load="1shv" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1shv, resolution 1.98&Aring;" />
 
-
'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''<br />
 
-
==Overview==
+
==STRUCTURE OF SHV-1 BETA-LACTAMASE==
-
The X-ray crystallographic structure of the SHV-1 beta-lactamase has been, established. The enzyme crystallizes from poly(ethylene glycol) at pH 7 in, space group P212121 with cell dimensions a = 49.6 A, b = 55.6 A, and c =, 87.0 A. The structure was solved by the molecular replacement method, and, the model has been refined to an R-factor of 0.18 for all data in the, range 8.0-1.98 A resolution. Deviations of model bonds and angles from, ideal values are 0.018 A and 1.8 degrees, respectively. Overlay of all 263, alpha-carbon atoms in the SHV-1 and TEM-1 beta-lactamases results in an, rms deviation of 1.4 A. Largest deviations occur in the H10 helix, (residues 218-224) and in the loops between strands in the beta-sheet. All, atoms in residues 70, 73, 130, 132, 166, and 234 in the catalytic site of, SHV-1 deviate only 0.23 A (rms) from atoms in TEM-1. However, the width of, the substrate binding cavity in SHV-1, as measured from the 104-105 and, 130-132 loops on one side to the 235-238 beta-strand on the other side, is, 0.7-1.2 A wider than in TEM-1. A structural analysis of the highly, different affinity of SHV-1 and TEM-1 for the beta-lactamase inhibitory, protein BLIP focuses on interactions involving Asp/Glu104.
+
<StructureSection load='1shv' size='340' side='right'caption='[[1shv]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1shv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHV 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]] 1.98&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</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=1shv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shv OCA], [https://pdbe.org/1shv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shv RCSB], [https://www.ebi.ac.uk/pdbsum/1shv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shv ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/BLA1_KLEPN BLA1_KLEPN]
 +
== 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/sh/1shv_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=1shv ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The X-ray crystallographic structure of the SHV-1 beta-lactamase has been established. The enzyme crystallizes from poly(ethylene glycol) at pH 7 in space group P212121 with cell dimensions a = 49.6 A, b = 55.6 A, and c = 87.0 A. The structure was solved by the molecular replacement method, and the model has been refined to an R-factor of 0.18 for all data in the range 8.0-1.98 A resolution. Deviations of model bonds and angles from ideal values are 0.018 A and 1.8 degrees, respectively. Overlay of all 263 alpha-carbon atoms in the SHV-1 and TEM-1 beta-lactamases results in an rms deviation of 1.4 A. Largest deviations occur in the H10 helix (residues 218-224) and in the loops between strands in the beta-sheet. All atoms in residues 70, 73, 130, 132, 166, and 234 in the catalytic site of SHV-1 deviate only 0.23 A (rms) from atoms in TEM-1. However, the width of the substrate binding cavity in SHV-1, as measured from the 104-105 and 130-132 loops on one side to the 235-238 beta-strand on the other side, is 0.7-1.2 A wider than in TEM-1. A structural analysis of the highly different affinity of SHV-1 and TEM-1 for the beta-lactamase inhibitory protein BLIP focuses on interactions involving Asp/Glu104.
-
==About this Structure==
+
Structure of the SHV-1 beta-lactamase.,Kuzin AP, Nukaga M, Nukaga Y, Hujer AM, Bonomo RA, Knox JR Biochemistry. 1999 May 4;38(18):5720-7. PMID:10231522<ref>PMID:10231522</ref>
-
1SHV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with MA4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SHV OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structure of the SHV-1 beta-lactamase., Kuzin AP, Nukaga M, Nukaga Y, Hujer AM, Bonomo RA, Knox JR, Biochemistry. 1999 May 4;38(18):5720-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10231522 10231522]
+
</div>
-
[[Category: Beta-lactamase]]
+
<div class="pdbe-citations 1shv" style="background-color:#fffaf0;"></div>
-
[[Category: Klebsiella pneumoniae]]
+
-
[[Category: Single protein]]
+
-
[[Category: Bonomo, R.A.]]
+
-
[[Category: Hujer, A.]]
+
-
[[Category: Knox, J.R.]]
+
-
[[Category: Kuzin, A.P.]]
+
-
[[Category: Nukaga, M.]]
+
-
[[Category: Nukaga, Y.]]
+
-
[[Category: MA4]]
+
-
[[Category: beta-lactam hydrolase]]
+
-
[[Category: detergent binding]]
+
-
[[Category: drug design]]
+
-
[[Category: penicillinase]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:23:42 2007''
+
==See Also==
 +
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Klebsiella pneumoniae]]
 +
[[Category: Large Structures]]
 +
[[Category: Bonomo RA]]
 +
[[Category: Hujer A]]
 +
[[Category: Knox JR]]
 +
[[Category: Kuzin AP]]
 +
[[Category: Nukaga M]]
 +
[[Category: Nukaga Y]]

Current revision

STRUCTURE OF SHV-1 BETA-LACTAMASE

PDB ID 1shv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1shv"
Personal tools