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.


1m7z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1m7z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m7z, resolution 2.14&Aring;" /> '''Structure of Nitric ...)
Current revision (07:41, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1m7z.gif|left|200px]]<br /><applet load="1m7z" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1m7z, resolution 2.14&Aring;" />
 
-
'''Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound'''<br />
 
-
==Overview==
+
==Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound==
-
Eukaryotic nitric oxide synthases (NOSs) produce nitric oxide to mediate, intercellular signaling and protect against pathogens. Recently, proteins, homologous to mammalian NOS oxygenase domains have been found in, prokaryotes and one from Bacillus subtilis (bsNOS) has been demonstrated, to produce nitric oxide [Adak, S., Aulak, K. S., and Stuehr, D. J. (2002), J. Biol. Chem. 277, 16167-16171]. We present structures of bsNOS complexed, with the active cofactor tetrahydrofolate and the substrate L-arginine, (L-Arg) or the intermediate N(omega)-hydroxy-L-arginine (NHA) to 1.9 or, 2.2 A resolution, respectively. The bsNOS structure is similar to those of, the mammalian NOS oxygenase domains (mNOS(ox)) except for the absence of, an N-terminal beta-hairpin hook and zinc-binding region that interact with, pterin and stabilize the mNOS(ox) dimer. Changes in patterns of residue, conservation between bacterial and mammalian NOSs correlate to different, binding modes for pterin side chains. Residue conservation on a surface, patch surrounding an exposed heme edge indicates a likely interaction site, for reductase proteins in all NOSs. The heme pockets of bsNOS and mNOS(ox), recognize L-Arg and NHA similarly, although a change from Val to Ile, beside the substrate guanidinium may explain the 10-20-fold slower, dissociation of product NO from the bacterial enzyme. Overall, these, structures suggest that bsNOS functions naturally to produce nitrogen, oxides from L-Arg and NHA in a pterin-dependent manner, but that the, regulation and purpose of NO production by NOS may be quite different in, B. subtilis than in mammals.
+
<StructureSection load='1m7z' size='340' side='right'caption='[[1m7z]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1m7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7Z 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]] 2.14&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HAR:N-OMEGA-HYDROXY-L-ARGININE'>HAR</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=1m7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7z OCA], [https://pdbe.org/1m7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7z RCSB], [https://www.ebi.ac.uk/pdbsum/1m7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7z ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NOSO_BACSU NOSO_BACSU] Catalyzes the production of nitric oxide.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/1m7z_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m7z ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1M7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with HEM, HAR and THG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M7Z OCA].
+
*[[Nitric Oxide Synthase 3D structures|Nitric Oxide Synthase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of a nitric oxide synthase heme protein from Bacillus subtilis., Pant K, Bilwes AM, Adak S, Stuehr DJ, Crane BR, Biochemistry. 2002 Sep 17;41(37):11071-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12220171 12220171]
+
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Nitric-oxide synthase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Adak S]]
-
[[Category: Adak, S.]]
+
[[Category: Bilwes AM]]
-
[[Category: Bilwes, A.M.]]
+
[[Category: Crane BR]]
-
[[Category: Crane, B.R.]]
+
[[Category: Pant K]]
-
[[Category: Pant, K.]]
+
[[Category: Stuehr DJ]]
-
[[Category: Stuehr, D.J.]]
+
-
[[Category: HAR]]
+
-
[[Category: HEM]]
+
-
[[Category: THG]]
+
-
[[Category: bacteria]]
+
-
[[Category: heme]]
+
-
[[Category: hydroxy arginine]]
+
-
[[Category: oxygenase]]
+
-
[[Category: pterin]]
+
-
[[Category: tetrahydrofolate]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:13:07 2007''
+

Current revision

Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound

PDB ID 1m7z

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/1m7z"
Personal tools