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.


3w1o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:43, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3w1o' size='340' side='right'caption='[[3w1o]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3w1o' size='340' side='right'caption='[[3w1o]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3w1o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1O FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3w1o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1O FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.85&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB2123 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3w1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1o OCA], [https://pdbe.org/3w1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1o RCSB], [https://www.ebi.ac.uk/pdbsum/3w1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1o ProSAT]</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=3w1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1o OCA], [https://pdbe.org/3w1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1o RCSB], [https://www.ebi.ac.uk/pdbsum/3w1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1o ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q9JXC6_NEIMB Q9JXC6_NEIMB]
-
DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical protein DMP12 should be added to this list. Our gel filtration and analytical ultracentrifugation results showed that the DMP12 monomer interacts with the dimeric form of the bacterial histone-like protein HU. Subsequent structural analysis of DMP12 showed that the shape and electrostatic surface of the DMP12 monomer are similar to those of the straight portion of the bent HU-bound DNA and complementary to those of HU protein dimer. DMP12 also protects HU protein from limited digestion by trypsin and enhances the growth rate Escherichia coli. Functionally, HU proteins participate in bacterial nucleoid formation, as well as recombination, gene regulation and DNA replication. The interaction between DMP12 and HU protein might, therefore, play important roles in these DNA-related mechanisms.
+
-
 
+
-
Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein.,Wang HC, Wu ML, Ko TP, Wang AH Nucleic Acids Res. 2013 Mar 26. PMID:23531546<ref>PMID:23531546</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3w1o" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Neimb]]
+
[[Category: Neisseria meningitidis MC58]]
-
[[Category: Ko, T P]]
+
[[Category: Ko TP]]
-
[[Category: Wang, A H.J]]
+
[[Category: Wang AHJ]]
-
[[Category: Wang, H C]]
+
[[Category: Wang HC]]
-
[[Category: Wu, M L]]
+
[[Category: Wu ML]]
-
[[Category: Dna mimic]]
+
-
[[Category: Hu protein]]
+
-
[[Category: Protein binding]]
+

Current revision

Neisseria DNA mimic protein DMP12

PDB ID 3w1o

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/3w1o"
Personal tools