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.


5u7c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:25, 6 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of the lead-bound form of MerB formed from diethyllead.==
==Crystal structure of the lead-bound form of MerB formed from diethyllead.==
-
<StructureSection load='5u7c' size='340' side='right' caption='[[5u7c]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+
<StructureSection load='5u7c' size='340' side='right'caption='[[5u7c]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5u7c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U7C FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5u7c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U7C FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=ZN7:DIETHYLLEAD+DIBROMIDE'>ZN7</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]] 1.75&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f0p|3f0p]], [[5c17|5c17]], [[5u7a|5u7a]], [[5u7b|5u7b]], [[5u79|5u79]], [[5u82|5u82]], [[5u83|5u83]], [[5u88|5u88]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=ZN7:DIETHYLLEAD+DIBROMIDE'>ZN7</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylmercury_lyase Alkylmercury lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.2 4.99.1.2] </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=5u7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u7c OCA], [https://pdbe.org/5u7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u7c RCSB], [https://www.ebi.ac.uk/pdbsum/5u7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u7c ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u7c OCA], [http://pdbe.org/5u7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u7c RCSB], [http://www.ebi.ac.uk/pdbsum/5u7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u7c ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/MERB_ECOLX MERB_ECOLX]] Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity).
+
[https://www.uniprot.org/uniprot/MERB_ECOLX MERB_ECOLX] Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity).
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The organomercurial lyase MerB has the unique ability to cleave carbon-Hg bonds, and structural studies indicate that three residues in the active site (C96, D99, and C159 in E. coli MerB) play important roles in the carbon-Hg bond cleavage. However, the role of each residue in carbon-metal bond cleavage has not been well-defined. To do so, we have structurally and biophysically characterized the interaction of MerB with a series of organotin and organolead compounds. Studies with two known inhibitors of MerB, dimethyltin (DMT) and triethyltin (TET), reveal that they inhibit by different mechanisms. In both cases the initial binding is to D99, but DMT subsequently binds to C96, which induces a conformation change in the active site. In contrast, diethyltin (DET) is a substrate for MerB and the SnIV product remains bound in the active site in a coordination similar to that of HgII following cleavage of organomercurial compounds. The results with analogous organolead compounds are similar in that trimethyllead (TML) is not cleaved and binds only to D99, whereas diethyllead (DEL) is a substrate and the PbIV product remains bound in the active site. Binding and cleavage is an exothermic reaction, while binding to D99 has negligible net heat flow. These results show that initial binding of organometallic compounds to MerB occurs at D99 followed, in some cases, by cleavage and loss of the organic moieties and binding of the metal ion product to C96, D99, and C159. The N-terminus of MerA is able to extract the bound PbVI but not the bound SnIV. These results suggest that MerB could be utilized for bioremediation applications, but certain organolead and organotin compounds may present an obstacle by inhibiting the enzyme.
+
-
 
+
-
Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase MerB Provide New Insights into Its Mechanism of Carbon-Metal Bond Cleavage.,Wahba HM, Stevenson MJ, Mansour A, Sygusch J, Wilcox DE, Omichinski JG J Am Chem Soc. 2017 Jan 3. doi: 10.1021/jacs.6b11327. PMID:27989130<ref>PMID:27989130</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5u7c" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Alkylmercury lyase]]
 
-
[[Category: Mansour, A]]
 
-
[[Category: Omichinski, J G]]
 
-
[[Category: Stevenson, M]]
 
-
[[Category: Sygusch, J]]
 
-
[[Category: Wahba, H M]]
 
-
[[Category: Wilcox, D E]]
 
-
[[Category: Bacterial protein]]
 
-
[[Category: Cysteine]]
 
-
[[Category: Diethyllead]]
 
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Lyase]]
+
[[Category: Large Structures]]
-
[[Category: Mercury]]
+
[[Category: Mansour A]]
-
[[Category: Metal binding protein]]
+
[[Category: Omichinski JG]]
 +
[[Category: Stevenson M]]
 +
[[Category: Sygusch J]]
 +
[[Category: Wahba HM]]
 +
[[Category: Wilcox DE]]

Current revision

Crystal structure of the lead-bound form of MerB formed from diethyllead.

PDB ID 5u7c

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/5u7c"
Personal tools