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.


4mda

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
<StructureSection load='4mda' size='340' side='right' caption='[[4mda]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4mda' size='340' side='right' caption='[[4mda]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4mda]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Droma Droma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDA OCA]. <br>
+
<table><tr><td colspan='2'>[[4mda]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Droma Droma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MDA FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=RLT:N-(4-FLUOROBENZYL)-5-HYDROXY-1-METHYL-2-(1-METHYL-1-{[(5-METHYL-1,3,4-OXADIAZOL-2-YL)CARBONYL]AMINO}ETHYL)-6-OXO-1,6-DIHYDROPYRIMIDINE-4-CARBOXAMIDE'>RLT</scene><br>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=RLT:N-(4-FLUOROBENZYL)-5-HYDROXY-1-METHYL-2-(1-METHYL-1-{[(5-METHYL-1,3,4-OXADIAZOL-2-YL)CARBONYL]AMINO}ETHYL)-6-OXO-1,6-DIHYDROPYRIMIDINE-4-CARBOXAMIDE'>RLT</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mdb|4mdb]], [[2f7t|2f7t]], [[3hos|3hos]], [[3hot|3hot]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mdb|4mdb]], [[2f7t|2f7t]], [[3hos|3hos]], [[3hot|3hot]]</td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mariner\T ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7226 DROMA])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mariner\T ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7226 DROMA])</td></tr>
-
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=4mda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mda RCSB], [http://www.ebi.ac.uk/pdbsum/4mda PDBsum]</span></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mda RCSB], [http://www.ebi.ac.uk/pdbsum/4mda PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
 +
[[http://www.uniprot.org/uniprot/MOS1T_DROMA MOS1T_DROMA]] Mediates transposition of transposon Mos1 by a 'cut and paste' mechanism. Transposases are sequence-specific nucleases and strand transferases that catalyze transposition through an ordered series of events: sequence-specific binding of transposase to the terminal inverted repeats (IR) present at each end of the transposon, pairing of the transposon IRs in a paired-end complex (PEC), cleavage of one or both DNA strands at each transposon end, capture of target DNA, and strand transfer to insert the transposon at a new site.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 15: Line 16:
Structural Basis of Mos1 Transposase Inhibition by the Anti-retroviral Drug Raltegravir.,Wolkowicz UM, Morris ER, Robson M, Trubitsyna M, Richardson JM ACS Chem Biol. 2014 Jan 10. PMID:24397848<ref>PMID:24397848</ref>
Structural Basis of Mos1 Transposase Inhibition by the Anti-retroviral Drug Raltegravir.,Wolkowicz UM, Morris ER, Robson M, Trubitsyna M, Richardson JM ACS Chem Biol. 2014 Jan 10. PMID:24397848<ref>PMID:24397848</ref>
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
 +
==See Also==
 +
*[[Transposase|Transposase]]
== References ==
== References ==
<references/>
<references/>
Line 22: Line 26:
</StructureSection>
</StructureSection>
[[Category: Droma]]
[[Category: Droma]]
-
[[Category: Richardson, J M.]]
+
[[Category: Richardson, J M]]
[[Category: Ddd motif]]
[[Category: Ddd motif]]
[[Category: Dna integration]]
[[Category: Dna integration]]

Revision as of 13:37, 24 December 2014

Structure of Mos1 transposase catalytic domain and Raltegravir with Mn

4mda, resolution 1.70Å

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/4mda"
Personal tools