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.

3mvf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:30, 25 December 2014

Crystal Structure of Nitrophorin 4 from Rhodnius prolixus Complexed with Nitrite at pH 7.4

Structural highlights

3mvf is a 1 chain structure with sequence from Rhodnius prolixus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The interaction of ferriheme proteins with nitrite has recently gained interest as a source for NO or other nitrogen oxides in mammalian physiology. However, met-hemoglobin (metHb), which was suggested as a key player in this process, does not convert nitrite unless small amounts of NO are added in parallel. We have recently reported that, in contrast, nitrophorins (NPs) convert nitrite as the sole substrate to form NO even at pH 7.5, which is an unprecedented case among ferrihemes [He, C., Knipp, M. (2009) J. Am. Chem. Soc. 131, 12042-12043]. NPs, which comprise a class of unique heme b proteins from the saliva of the blood feeding insect Rhodnius prolixus, appear in a number of concomitant isoproteins. Herein, the first spectroscopic characterization of the initial complexes of the two isoproteins NP4 and NP7 with nitrite is presented and compared to the data reported for metHb and met-myoglobin (metMb). Because upon nitrite binding, NPs, in contrast to metHb and metMb, continue to react with nitrite, resonance Raman spectroscopy and cw-EPR spectroscopy were applied to frozen samples. As a result, the existence of two 6-coordinate ferriheme low-spin complexes was established. Furthermore, X-ray crystallography of NP4 crystals soaked with nitrite revealed the formation of a eta1-N nitro complex, which is in contrast to the eta1-O bound nitrite in metMb and metHb. Stopped-flow kinetic experiments show that although the ligand dissociation constants of NP4 and NP7 (15 to 190 M horizontal line 1) are comparable to those of the metHb and metMb, the rates of ligand binding and release are significantly slower. Moreover, the reaction kinetics, but also EPR spectroscopy exhibits notable differences between the two isoproteins.

Complex Formation of Nitrite with the Ferriheme b beta-Barrel Proteins Nitrophorin 4 and Nitrophorin 7.,He C, Ogata H, Knipp M Biochemistry. 2010 Jun 4. PMID:20524697^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ He C, Ogata H, Knipp M. Complex Formation of Nitrite with the Ferriheme b beta-Barrel Proteins Nitrophorin 4 and Nitrophorin 7. Biochemistry. 2010 Jun 4. PMID:20524697 doi:10.1021/bi100324z

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mvf"

@@ Line 6: / Line 6: @@
 <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=3mvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mvf RCSB], [http://www.ebi.ac.uk/pdbsum/3mvf PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3mvf

From Proteopedia

Revision as of 13:30, 25 December 2014

Crystal Structure of Nitrophorin 4 from Rhodnius prolixus Complexed with Nitrite at pH 7.4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox