View source for 3tga


==Crystal structure of L130R mutant of Nitrophorin 4 from Rhodnius prolixus at pH 7.4==
<StructureSection load='3tga' size='340' side='right'caption='[[3tga]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tga]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TGA 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]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=3tga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tga OCA], [https://pdbe.org/3tga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tga RCSB], [https://www.ebi.ac.uk/pdbsum/3tga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tga ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NP4_RHOPR NP4_RHOPR] Heme-based protein that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing (By similarity).
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== Publication Abstract from PubMed ==
Prestidigitation: In a mutant of the heme protein nitrophorin 4, the first binding of guanidine to iron in a porphyrin is observed. The protein pocket has two effects that aid this binding: its overall structure holds the ligands together providing binding energy from the chelate effect and it facilitates the deprotonation of the highly basic guanidine residue.

Guanidine-Ferroheme Coordination in the Mutant Protein Nitrophorin 4(L130R).,He C, Fuchs MR, Ogata H, Knipp M Angew Chem Int Ed Engl. 2012 Apr 27;51(18):4470-3. doi: 10.1002/anie.201108691., Epub 2012 Feb 14. PMID:22334402<ref>PMID:22334402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3tga" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitrophorin|Nitrophorin]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodnius prolixus]]
[[Category: He C]]
[[Category: Knipp M]]
[[Category: Ogata H]]